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Siroheme synthase [Includes: Sirohydrochlorin ferrochelatase (EC 4.99.1.4); Precorrin-2 dehydrogenase (EC 1.3.1.76); Uroporphyrinogen-III C-methyltransferase (Urogen III methylase) (EC 2.1.1.107) (Uroporphyrinogen III methylase) (UROM) (SUMT)]

 K1ISI7_9GAMM            Unreviewed;       463 AA.
K1ISI7;
28-NOV-2012, integrated into UniProtKB/TrEMBL.
28-NOV-2012, sequence version 1.
30-AUG-2017, entry version 37.
RecName: Full=Siroheme synthase {ECO:0000256|HAMAP-Rule:MF_01646};
Includes:
RecName: Full=Uroporphyrinogen-III C-methyltransferase {ECO:0000256|HAMAP-Rule:MF_01646};
Short=Urogen III methylase {ECO:0000256|HAMAP-Rule:MF_01646};
EC=2.1.1.107 {ECO:0000256|HAMAP-Rule:MF_01646};
AltName: Full=Uroporphyrinogen III methylase {ECO:0000256|HAMAP-Rule:MF_01646};
Short=UROM {ECO:0000256|HAMAP-Rule:MF_01646};
AltName: Full=SUMT {ECO:0000256|HAMAP-Rule:MF_01646};
Includes:
RecName: Full=Sirohydrochlorin ferrochelatase {ECO:0000256|HAMAP-Rule:MF_01646};
EC=4.99.1.4 {ECO:0000256|HAMAP-Rule:MF_01646};
Includes:
RecName: Full=Precorrin-2 dehydrogenase {ECO:0000256|HAMAP-Rule:MF_01646};
EC=1.3.1.76 {ECO:0000256|HAMAP-Rule:MF_01646};
Name=cysG {ECO:0000256|HAMAP-Rule:MF_01646};
ORFNames=HMPREF1168_02546 {ECO:0000313|EMBL:EKB18772.1};
Aeromonas veronii AMC34.
Bacteria; Proteobacteria; Gammaproteobacteria; Aeromonadales;
Aeromonadaceae; Aeromonas.
NCBI_TaxID=1073383 {ECO:0000313|EMBL:EKB18772.1, ECO:0000313|Proteomes:UP000006087};
[1] {ECO:0000313|EMBL:EKB18772.1, ECO:0000313|Proteomes:UP000006087}
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=AMC34 {ECO:0000313|EMBL:EKB18772.1,
ECO:0000313|Proteomes:UP000006087};
The Broad Institute Genome Sequencing Platform;
Earl A., Ward D., Feldgarden M., Gevers D., Graf J., Tomasi A.,
Horneman A., Walker B., Young S.K., Zeng Q., Gargeya S.,
Fitzgerald M., Haas B., Abouelleil A., Alvarado L., Arachchi H.M.,
Berlin A.M., Chapman S.B., Goldberg J., Griggs A., Gujja S.,
Hansen M., Howarth C., Imamovic A., Larimer J., McCowan C.,
Montmayeur A., Murphy C., Neiman D., Pearson M., Priest M.,
Roberts A., Saif S., Shea T., Sisk P., Sykes S., Wortman J.,
Nusbaum C., Birren B.;
"The Genome Sequence of Aeromonas veronii AMC34.";
Submitted (JUN-2012) to the EMBL/GenBank/DDBJ databases.
-!- FUNCTION: Multifunctional enzyme that catalyzes the SAM-dependent
methylations of uroporphyrinogen III at position C-2 and C-7 to
form precorrin-2 via precorrin-1. Then it catalyzes the NAD-
dependent ring dehydrogenation of precorrin-2 to yield
sirohydrochlorin. Finally, it catalyzes the ferrochelation of
sirohydrochlorin to yield siroheme. {ECO:0000256|HAMAP-
Rule:MF_01646, ECO:0000256|SAAS:SAAS00240176}.
-!- CATALYTIC ACTIVITY: Precorrin-2 + NAD(+) = sirohydrochlorin +
NADH. {ECO:0000256|HAMAP-Rule:MF_01646,
ECO:0000256|SAAS:SAAS00324440}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + precorrin-1 = S-
adenosyl-L-homocysteine + precorrin-2. {ECO:0000256|HAMAP-
Rule:MF_01646, ECO:0000256|SAAS:SAAS00825977}.
-!- CATALYTIC ACTIVITY: S-adenosyl-L-methionine + uroporphyrinogen III
= S-adenosyl-L-homocysteine + precorrin-1. {ECO:0000256|HAMAP-
Rule:MF_01646, ECO:0000256|SAAS:SAAS00825997}.
-!- CATALYTIC ACTIVITY: Siroheme + 2 H(+) = sirohydrochlorin + Fe(2+).
{ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00240160}.
-!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
sirohydrochlorin from precorrin-2: step 1/1. {ECO:0000256|HAMAP-
Rule:MF_01646, ECO:0000256|SAAS:SAAS00350842}.
-!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
biosynthesis; precorrin-2 from uroporphyrinogen III: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00350909}.
-!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
biosynthesis; siroheme from sirohydrochlorin: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00350918}.
-!- PATHWAY: Porphyrin-containing compound metabolism; siroheme
biosynthesis; sirohydrochlorin from precorrin-2: step 1/1.
{ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00324439}.
-!- SIMILARITY: Belongs to the precorrin methyltransferase family.
{ECO:0000256|RuleBase:RU003960}.
-!- SIMILARITY: In the C-terminal section; belongs to the precorrin
methyltransferase family. {ECO:0000256|HAMAP-Rule:MF_01646,
ECO:0000256|SAAS:SAAS00545078}.
-!- SIMILARITY: In the N-terminal section; belongs to the precorrin-2
dehydrogenase / sirohydrochlorin ferrochelatase family.
{ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00545089}.
-!- CAUTION: The sequence shown here is derived from an
EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
preliminary data. {ECO:0000313|EMBL:EKB18772.1}.
-----------------------------------------------------------------------
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EMBL; AGWU01000020; EKB18772.1; -; Genomic_DNA.
RefSeq; WP_005344959.1; NZ_JH823256.1.
EnsemblBacteria; EKB18772; EKB18772; HMPREF1168_02546.
PATRIC; fig|1073383.3.peg.2566; -.
UniPathway; UPA00148; UER00222.
UniPathway; UPA00262; UER00211.
UniPathway; UPA00262; UER00222.
UniPathway; UPA00262; UER00376.
Proteomes; UP000006087; Unassembled WGS sequence.
GO; GO:0051287; F:NAD binding; IEA:InterPro.
GO; GO:0043115; F:precorrin-2 dehydrogenase activity; IEA:UniProtKB-HAMAP.
GO; GO:0051266; F:sirohydrochlorin ferrochelatase activity; IEA:UniProtKB-EC.
GO; GO:0004851; F:uroporphyrin-III C-methyltransferase activity; IEA:UniProtKB-HAMAP.
GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-HAMAP.
GO; GO:0019354; P:siroheme biosynthetic process; IEA:UniProtKB-HAMAP.
Gene3D; 1.10.8.210; -; 1.
Gene3D; 3.30.950.10; -; 1.
Gene3D; 3.40.1010.10; -; 1.
HAMAP; MF_01646; Siroheme_synth; 1.
InterPro; IPR000878; 4pyrrol_Mease.
InterPro; IPR014777; 4pyrrole_Mease_sub1.
InterPro; IPR014776; 4pyrrole_Mease_sub2.
InterPro; IPR006366; CobA/CysG_C.
InterPro; IPR016040; NAD(P)-bd_dom.
InterPro; IPR012409; Sirohaem_synth.
InterPro; IPR028281; Sirohaem_synthase_central.
InterPro; IPR019478; Sirohaem_synthase_dimer_dom.
InterPro; IPR006367; Sirohaem_synthase_N.
InterPro; IPR003043; Uropor_MeTrfase_CS.
Pfam; PF10414; CysG_dimeriser; 1.
Pfam; PF13241; NAD_binding_7; 1.
Pfam; PF14824; Sirohm_synth_M; 1.
Pfam; PF00590; TP_methylase; 1.
PIRSF; PIRSF036426; Sirohaem_synth; 1.
SUPFAM; SSF51735; SSF51735; 1.
SUPFAM; SSF53790; SSF53790; 1.
TIGRFAMs; TIGR01469; cobA_cysG_Cterm; 1.
TIGRFAMs; TIGR01470; cysG_Nterm; 1.
PROSITE; PS00840; SUMT_2; 1.
3: Inferred from homology;
Cobalamin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01646,
ECO:0000256|SAAS:SAAS00025873};
Complete proteome {ECO:0000313|Proteomes:UP000006087};
Lyase {ECO:0000256|HAMAP-Rule:MF_01646,
ECO:0000256|SAAS:SAAS00025919};
Methyltransferase {ECO:0000256|HAMAP-Rule:MF_01646,
ECO:0000256|RuleBase:RU003960, ECO:0000256|SAAS:SAAS00099290};
Multifunctional enzyme {ECO:0000256|HAMAP-Rule:MF_01646,
ECO:0000256|SAAS:SAAS00428961};
NAD {ECO:0000256|HAMAP-Rule:MF_01646, ECO:0000256|SAAS:SAAS00324437};
Oxidoreductase {ECO:0000256|HAMAP-Rule:MF_01646,
ECO:0000256|SAAS:SAAS00324475};
Phosphoprotein {ECO:0000256|HAMAP-Rule:MF_01646};
Porphyrin biosynthesis {ECO:0000256|HAMAP-Rule:MF_01646,
ECO:0000256|SAAS:SAAS00324438};
S-adenosyl-L-methionine {ECO:0000256|HAMAP-Rule:MF_01646,
ECO:0000256|SAAS:SAAS00099242};
Transferase {ECO:0000256|HAMAP-Rule:MF_01646,
ECO:0000256|RuleBase:RU003960, ECO:0000256|SAAS:SAAS00099290}.
DOMAIN 6 115 NAD_binding_7.
{ECO:0000259|Pfam:PF13241}.
DOMAIN 119 146 Sirohm_synth_M.
{ECO:0000259|Pfam:PF14824}.
DOMAIN 150 207 CysG_dimeriser.
{ECO:0000259|Pfam:PF10414}.
DOMAIN 217 427 TP_methylase. {ECO:0000259|Pfam:PF00590}.
NP_BIND 22 23 NAD. {ECO:0000256|HAMAP-Rule:MF_01646}.
NP_BIND 43 44 NAD. {ECO:0000256|HAMAP-Rule:MF_01646}.
REGION 1 203 precorrin-2 dehydrogenase /
sirohydrochlorin ferrochelatase.
{ECO:0000256|HAMAP-Rule:MF_01646}.
REGION 215 463 Uroporphyrinogen-III C-methyltransferase.
{ECO:0000256|HAMAP-Rule:MF_01646}.
REGION 300 302 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_01646}.
REGION 330 331 S-adenosyl-L-methionine binding.
{ECO:0000256|HAMAP-Rule:MF_01646}.
ACT_SITE 247 247 Proton acceptor. {ECO:0000256|HAMAP-
Rule:MF_01646,
ECO:0000256|PIRSR:PIRSR036426-1}.
ACT_SITE 269 269 Proton donor. {ECO:0000256|HAMAP-
Rule:MF_01646,
ECO:0000256|PIRSR:PIRSR036426-1}.
BINDING 224 224 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_01646}.
BINDING 305 305 S-adenosyl-L-methionine; via carbonyl
oxygen. {ECO:0000256|HAMAP-
Rule:MF_01646}.
BINDING 382 382 S-adenosyl-L-methionine; via amide
nitrogen. {ECO:0000256|HAMAP-
Rule:MF_01646}.
BINDING 411 411 S-adenosyl-L-methionine; via amide
nitrogen and carbonyl oxygen.
{ECO:0000256|HAMAP-Rule:MF_01646}.
MOD_RES 128 128 Phosphoserine. {ECO:0000256|HAMAP-
Rule:MF_01646}.
SEQUENCE 463 AA; 50198 MW; 36DC544ADA6687F9 CRC64;
MDFLPLFCQL QNKPVLIVGG GEVAVRKARL LLDAKAKITI NSPHLEPQLM SWAEQGRLTV
CAAGFHPELL DGKWLVIAAT NQPEVNQQVF NEASLRQIFC NVVDSPAHCS AIMPAIIDRS
PLMVAISSAG AAPVLSRQLR EKFEAMLPQH LGQLAALAGK LRERVKAIPD KLARRRFWER
LFSHERLACQ LARGQQQAAE QSVAELLNEP VLSKGSVTLV GAGPGDAGLL TLSGLQQLQQ
ADVVVYDRLV SQEVLALVRR DAERIFVGKE AGRHCVPQQA INQLLLEQAQ LGKQVVRLKG
GDPFIFGRGG EELETLAEAG IPFSVVPGIT AASGCAAYSG IPLTHRDHAQ RVQFITGHDK
EGNIAQEWST LAAPRQTLVF YMGLAHAARI QDELQTHGLP GHTPVALVEQ GTRLQQRVVR
GELQQLAQLA TQVDSPSLII IGSVVTLADK LDWYGEANTL AGV


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