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Globin-coupled histidine kinase (EC 2.7.13.3) (AfGcHK) (Heme-based oxygen-sensor histidine kinase)

 GCHK_ANADF              Reviewed;         382 AA.
A7HD43;
21-MAR-2012, integrated into UniProtKB/Swiss-Prot.
11-SEP-2007, sequence version 1.
25-APR-2018, entry version 71.
RecName: Full=Globin-coupled histidine kinase {ECO:0000303|PubMed:21852234};
EC=2.7.13.3 {ECO:0000269|PubMed:21852234, ECO:0000269|PubMed:26212354};
AltName: Full=AfGcHK {ECO:0000303|PubMed:21852234, ECO:0000303|PubMed:26212354};
AltName: Full=Heme-based oxygen-sensor histidine kinase {ECO:0000303|PubMed:21852234};
Name=gchK {ECO:0000303|PubMed:21852234};
OrderedLocusNames=Anae109_2438;
Anaeromyxobacter sp. (strain Fw109-5).
Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
Cystobacterineae; Anaeromyxobacteraceae; Anaeromyxobacter.
NCBI_TaxID=404589;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=Fw109-5;
PubMed=25614562; DOI=10.1128/genomeA.01449-14;
Hwang C., Copeland A., Lucas S., Lapidus A., Barry K.,
Glavina Del Rio T., Dalin E., Tice H., Pitluck S., Sims D.,
Brettin T., Bruce D.C., Detter J.C., Han C.S., Schmutz J.,
Larimer F.W., Land M.L., Hauser L.J., Kyrpides N., Lykidis A.,
Richardson P., Belieav A., Sanford R.A., Loeffler F.E., Fields M.W.;
"Complete genome sequence of Anaeromyxobacter sp. Fw109-5, an
anaerobic, metal-reducing bacterium isolated from a contaminated
subsurface environment.";
Genome Announc. 3:0-0(2015).
[2]
FUNCTION, CATALYTIC ACTIVITY, COFACTOR, ENZYME REGULATION,
HEME-BINDING, OXYGEN-BINDING, RESONANCE RAMAN SPECTROSCOPY, PTM,
PHOSPHORYLATION AT HIS-183, SUBUNIT, GENE NAME, MUTAGENESIS OF TYR-45;
HIS-99 AND HIS-183, AND DOMAIN.
STRAIN=Fw109-5;
PubMed=21852234; DOI=10.1074/jbc.M111.274811;
Kitanishi K., Kobayashi K., Uchida T., Ishimori K., Igarashi J.,
Shimizu T.;
"Identification and functional and spectral characterization of a
globin-coupled histidine kinase from Anaeromyxobacter sp. Fw109-5.";
J. Biol. Chem. 286:35522-35534(2011).
[3]
AUTOPHOSPHORYLATION ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, ENZYME
REGULATION, MUTAGENESIS OF HIS-99, AND DOMAIN.
STRAIN=Fw109-5;
PubMed=26212354; DOI=10.1021/acs.biochem.5b00517;
Fojtikova V., Stranava M., Vos M.H., Liebl U., Hranicek J.,
Kitanishi K., Shimizu T., Martinkova M.;
"Kinetic analysis of a globin-coupled histidine kinase, AfGcHK:
Effects of the heme iron complex, response regulator, and metal
cations on autophosphorylation activity.";
Biochemistry 54:5017-5029(2015).
-!- FUNCTION: Member of the two-component regulatory system
GcHK/Anae109_2439. Autophosphorylates in response to oxygen
availability, and then transfers the phosphate group to a
conserved Asp residue in the receiver domains of the cognate
response regulator Anae109_2439, resulting in its activation.
{ECO:0000269|PubMed:21852234}.
-!- CATALYTIC ACTIVITY: ATP + protein L-histidine = ADP + protein N-
phospho-L-histidine. {ECO:0000269|PubMed:21852234,
ECO:0000269|PubMed:26212354}.
-!- COFACTOR:
Name=heme b; Xref=ChEBI:CHEBI:60344;
Evidence={ECO:0000269|PubMed:21852234};
Note=Binds 1 heme b (iron(II)-protoporphyrin IX) group per
subunit. {ECO:0000269|PubMed:21852234};
-!- ENZYME REGULATION: Gas or ligand binding and heme iron redox state
regulate the histidine kinase activity: heme-free AfGcHK and the
heme Fe(II) complex are less active forms, whereas the heme
Fe(III)-OH(-), Fe(III)-CN(-), Fe(III)-imidazole, Fe(II)-CO, and
Fe(II)-O(2) complexes are active forms. The activation of the
functional domain seems to be dependent on the formation of a six-
coordinate low-spin heme iron complex. Mg(2+) ions, and to a
lesser extent, Mn(2+) ions, enhance the autophosphorylation
reaction, although the presence of a divalent metal ion does not
appear to be essential for the reaction. Co(2+), Ni(2+), Zn(2+),
and Cd(2+) totally inhibit autophosphorylation activity.
{ECO:0000269|PubMed:21852234, ECO:0000269|PubMed:26212354}.
-!- BIOPHYSICOCHEMICAL PROPERTIES:
Kinetic parameters:
KM=18.9 uM for ATP (with the Fe(III)-OH(-) bound form of the
enzyme) {ECO:0000269|PubMed:26212354};
KM=35.4 uM for ATP (with the Fe(III)-CN(-) bound form of the
enzyme) {ECO:0000269|PubMed:26212354};
KM=23.8 uM for ATP (with the Fe(III)-imidazole bound form of the
enzyme) {ECO:0000269|PubMed:26212354};
KM=23.0 uM for ATP (with the Fe(II)-O(2) bound form of the
enzyme) {ECO:0000269|PubMed:26212354};
KM=357.0 uM for ATP (with the Fe(II)-CO bound form of the
enzyme) {ECO:0000269|PubMed:26212354};
KM=78 uM for ATP (with the Fe(II) bound form of the enzyme)
{ECO:0000269|PubMed:26212354};
KM=33.6 uM for ATP (with the heme-free form of the enzyme)
{ECO:0000269|PubMed:26212354};
Note=kcat is 1.1 min(-1) for the autophosphorylation reaction
with the Fe(III)-OH(-) bound form of the enzyme. kcat is 1.2
min(-1) with the Fe(III)-CN(-) bound form of the enzyme. kcat is
1.1 min(-1) with the Fe(III)-imidazole bound form of the enzyme.
kcat is 1.0 min(-1) with the Fe(II)-O(2) bound form of the
enzyme. kcat is 1.0 min(-1) with the Fe(II)-CO bound form of the
enzyme. kcat is 0.4 min(-1) with the Fe(II) bound form of the
enzyme. kcat is 0.3 min(-1) with the heme-free form of the
enzyme. The presence of the cognate response regulator (RR)
protein significantly reduces the enzyme affinity for ATP.
{ECO:0000269|PubMed:26212354};
pH dependence:
Optimum pH is around 11.0 for the autophosphorylation reaction
with the Fe(III)-OH(-) bound form of the enzyme. At pH 8.0,
displays 75% of the optimal rate. Is inactive below pH 5.5 and
above pH 12.7. {ECO:0000269|PubMed:26212354};
-!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:21852234}.
-!- DOMAIN: Consists of two domains: an N-terminal heme-based oxygen-
sensor domain, and a C-terminal catalytic domain that exhibits
histidine kinase activity (PubMed:21852234). The coordination and
oxidation state of the sensor domain heme iron profoundly affect
the enzyme's catalytic activity (PubMed:26212354).
{ECO:0000269|PubMed:26212354, ECO:0000305|PubMed:21852234}.
-!- PTM: Autophosphorylated. {ECO:0000269|PubMed:21852234,
ECO:0000269|PubMed:26212354}.
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EMBL; CP000769; ABS26639.1; -; Genomic_DNA.
PDB; 5OHE; X-ray; 1.85 A; A/B/C/D/E/F/G/H=2-161.
PDB; 5OHF; X-ray; 1.80 A; A/B/C/D/E/F/G/H=2-161.
PDBsum; 5OHE; -.
PDBsum; 5OHF; -.
ProteinModelPortal; A7HD43; -.
SMR; A7HD43; -.
STRING; 404589.Anae109_2438; -.
iPTMnet; A7HD43; -.
EnsemblBacteria; ABS26639; ABS26639; Anae109_2438.
KEGG; afw:Anae109_2438; -.
eggNOG; ENOG4108TQ9; Bacteria.
eggNOG; COG0642; LUCA.
HOGENOM; HOG000003231; -.
OMA; IETSLYI; -.
OrthoDB; POG091H03OF; -.
SABIO-RK; A7HD43; -.
Proteomes; UP000006382; Chromosome.
GO; GO:0005622; C:intracellular; IEA:GOC.
GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
GO; GO:0020037; F:heme binding; IDA:UniProtKB.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0019825; F:oxygen binding; IDA:UniProtKB.
GO; GO:0000155; F:phosphorelay sensor kinase activity; IDA:UniProtKB.
GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
GO; GO:0018106; P:peptidyl-histidine phosphorylation; IDA:UniProtKB.
GO; GO:0000160; P:phosphorelay signal transduction system; IDA:UniProtKB.
CDD; cd00075; HATPase_c; 1.
CDD; cd00082; HisKA; 1.
Gene3D; 1.10.490.10; -; 1.
Gene3D; 3.30.565.10; -; 1.
InterPro; IPR009050; Globin-like_sf.
InterPro; IPR012292; Globin/Proto.
InterPro; IPR003594; HATPase_C.
InterPro; IPR036890; HATPase_C_sf.
InterPro; IPR005467; His_kinase_dom.
InterPro; IPR003661; HisK_dim/P.
InterPro; IPR036097; HisK_dim/P_sf.
InterPro; IPR004358; Sig_transdc_His_kin-like_C.
Pfam; PF02518; HATPase_c; 1.
Pfam; PF00512; HisKA; 1.
PRINTS; PR00344; BCTRLSENSOR.
SMART; SM00387; HATPase_c; 1.
SMART; SM00388; HisKA; 1.
SUPFAM; SSF46458; SSF46458; 1.
SUPFAM; SSF47384; SSF47384; 1.
SUPFAM; SSF55874; SSF55874; 1.
PROSITE; PS50109; HIS_KIN; 1.
1: Evidence at protein level;
3D-structure; ATP-binding; Complete proteome; Heme; Iron; Kinase;
Metal-binding; Nucleotide-binding; Phosphoprotein; Reference proteome;
Transferase; Two-component regulatory system.
CHAIN 1 382 Globin-coupled histidine kinase.
/FTId=PRO_5000267182.
DOMAIN 180 382 Histidine kinase. {ECO:0000255|PROSITE-
ProRule:PRU00107,
ECO:0000305|PubMed:21852234}.
REGION 1 155 Globin sensor.
{ECO:0000305|PubMed:21852234}.
METAL 99 99 Iron (heme proximal ligand).
{ECO:0000269|PubMed:21852234}.
BINDING 45 45 Oxygen. {ECO:0000269|PubMed:21852234}.
MOD_RES 183 183 Phosphohistidine; by autocatalysis.
{ECO:0000255|PROSITE-ProRule:PRU00107,
ECO:0000269|PubMed:21852234}.
MUTAGEN 45 45 Y->F: 3.5-fold increase in O(2)
dissociation rate constant. No effect on
O(2) association rate constant.
{ECO:0000269|PubMed:21852234}.
MUTAGEN 45 45 Y->L: 80-fold increase in O(2)
dissociation rate constant. No effect on
O(2) association rate constant.
{ECO:0000269|PubMed:21852234}.
MUTAGEN 45 45 Y->W: 34-fold increase in O(2)
dissociation rate constant. No effect on
O(2) association rate constant.
{ECO:0000269|PubMed:21852234}.
MUTAGEN 99 99 H->A: Loss of heme-binding ability. 4-
fold decrease in autophosphorylation
reaction rate and 2-fold decrease in
affinity for ATP.
{ECO:0000269|PubMed:21852234,
ECO:0000269|PubMed:26212354}.
MUTAGEN 183 183 H->A: Loss of autophosphorylation. Does
not significantly alter the O(2) and CO
binding kinetic values.
{ECO:0000269|PubMed:21852234}.
HELIX 8 16 {ECO:0000244|PDB:5OHF}.
HELIX 20 33 {ECO:0000244|PDB:5OHF}.
HELIX 34 36 {ECO:0000244|PDB:5OHF}.
HELIX 37 49 {ECO:0000244|PDB:5OHF}.
HELIX 54 57 {ECO:0000244|PDB:5OHF}.
HELIX 61 81 {ECO:0000244|PDB:5OHF}.
HELIX 86 101 {ECO:0000244|PDB:5OHF}.
HELIX 107 128 {ECO:0000244|PDB:5OHF}.
HELIX 132 156 {ECO:0000244|PDB:5OHF}.
SEQUENCE 382 AA; 41941 MW; D007A082ABD1F8EA CRC64;
MTGVPETVFE ELKRYVGWGD GDERALRSLH GAAAPHFPRL AEEFYDRILG HEGARTALVG
GESQVGHLKV TMIAWLDELL GGPWDEAYWD RRYRIGRVHV RIGLPQHYMF GAMNVHRTGL
ARLAYERFHG DPPELERVRN ALGKVLDLEL AVMLHTYRED LLAQQARVER LSTFGQLVGS
IGHDLRNPLG VIETSLYILR TRTGEDERAR KHLDRIGEQL GVANGIITNL LDMIRDRPLA
REPVELAAVV GGAAESVRRP TGVSLALEGL DALPPVEGDP GQLRQVFVNL LENAVFAASP
EGVVAVRASR ADGLVALDVE DSGPGVDPAT RRRLFEPLIT TKDKGIGLGL ALVKRIAERH
GGTVEYSDRP GGGARFTVRL PA


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