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Aconitate hydratase B (EC 4.2.1.3) (EC 4.2.1.99) (2-methylisocitrate dehydratase)

 Q1PJ84_PROMR            Unreviewed;       857 AA.
Q1PJ84;
16-MAY-2006, integrated into UniProtKB/TrEMBL.
16-MAY-2006, sequence version 1.
15-MAR-2017, entry version 67.
RecName: Full=Aconitate hydratase B {ECO:0000256|PIRNR:PIRNR036687};
EC=4.2.1.3 {ECO:0000256|PIRNR:PIRNR036687};
EC=4.2.1.99 {ECO:0000256|PIRNR:PIRNR036687};
AltName: Full=2-methylisocitrate dehydratase {ECO:0000256|PIRNR:PIRNR036687};
Name=acnB {ECO:0000313|EMBL:ABE11498.1};
ORFNames=HOT0M-8F9_0015 {ECO:0000313|EMBL:ABE11498.1};
uncultured Prochlorococcus marinus clone HOT0M-8F9.
Bacteria; Cyanobacteria; Synechococcales; Prochloraceae;
Prochlorococcus.
NCBI_TaxID=379395 {ECO:0000313|EMBL:ABE11498.1};
[1] {ECO:0000313|EMBL:ABE11498.1}
NUCLEOTIDE SEQUENCE.
PubMed=16556843; DOI=10.1126/science.1122050;
Coleman M.L., Sullivan M.B., Martiny A.C., Steglich C., Barry K.,
Delong E.F., Chisholm S.W.;
"Genomic islands and the ecology and evolution of Prochlorococcus.";
Science 311:1768-1770(2006).
[2] {ECO:0000313|EMBL:ABE11498.1}
NUCLEOTIDE SEQUENCE.
US DOE Joint Genome Institute (JGI);
Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C., Glavina T.,
Hammon N., Israni S., Richardson P.;
"Sequencing of the draft fosmids and assembly of Prochlorococcus
marinus environmental genome fragment.";
Submitted (APR-2006) to the EMBL/GenBank/DDBJ databases.
-!- CATALYTIC ACTIVITY: (2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate =
(Z)-but-2-ene-1,2,3-tricarboxylate + H(2)O.
{ECO:0000256|PIRNR:PIRNR036687}.
-!- CATALYTIC ACTIVITY: Citrate = isocitrate.
{ECO:0000256|PIRNR:PIRNR036687}.
-!- COFACTOR:
Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
Evidence={ECO:0000256|PIRSR:PIRSR036687-1};
Note=Binds 1 [4Fe-4S] cluster per subunit.
{ECO:0000256|PIRSR:PIRSR036687-1};
-!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle;
isocitrate from oxaloacetate: step 2/2.
{ECO:0000256|PIRNR:PIRNR036687}.
-!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
{ECO:0000256|PIRNR:PIRNR036687}.
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EMBL; DQ366743; ABE11498.1; -; Genomic_DNA.
ProteinModelPortal; Q1PJ84; -.
UniPathway; UPA00223; UER00718.
GO; GO:0005829; C:cytosol; IEA:InterPro.
GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
CDD; cd01576; AcnB_Swivel; 1.
Gene3D; 3.20.19.10; -; 1.
Gene3D; 3.30.499.10; -; 2.
Gene3D; 3.40.1060.10; -; 1.
InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
InterPro; IPR015932; Aconitase/IPMdHydase_lsu_aba_2.
InterPro; IPR018136; Aconitase_4Fe-4S_BS.
InterPro; IPR004406; Aconitase_B.
InterPro; IPR015933; Aconitase_B_HEAT-like_dom.
InterPro; IPR015929; Aconitase_B_swivel.
PANTHER; PTHR43160:SF3; PTHR43160:SF3; 1.
Pfam; PF00330; Aconitase; 1.
Pfam; PF06434; Aconitase_2_N; 1.
Pfam; PF11791; Aconitase_B_N; 1.
PIRSF; PIRSF036687; AcnB; 1.
SUPFAM; SSF52016; SSF52016; 1.
SUPFAM; SSF53732; SSF53732; 1.
SUPFAM; SSF74778; SSF74778; 1.
TIGRFAMs; TIGR00117; acnB; 1.
PROSITE; PS00450; ACONITASE_1; 1.
PROSITE; PS01244; ACONITASE_2; 1.
3: Inferred from homology;
4Fe-4S {ECO:0000256|PIRSR:PIRSR036687-1,
ECO:0000256|SAAS:SAAS00640307};
Iron {ECO:0000256|PIRSR:PIRSR036687-1, ECO:0000256|SAAS:SAAS00640307};
Iron-sulfur {ECO:0000256|PIRSR:PIRSR036687-1,
ECO:0000256|SAAS:SAAS00640307};
Lyase {ECO:0000256|PIRNR:PIRNR036687, ECO:0000256|SAAS:SAAS00638284};
Metal-binding {ECO:0000256|PIRSR:PIRSR036687-1,
ECO:0000256|SAAS:SAAS00640307};
Tricarboxylic acid cycle {ECO:0000256|PIRNR:PIRNR036687}.
DOMAIN 10 163 Aconitase_B_N.
{ECO:0000259|Pfam:PF11791}.
DOMAIN 176 383 Aconitase_2_N.
{ECO:0000259|Pfam:PF06434}.
DOMAIN 471 818 Aconitase. {ECO:0000259|Pfam:PF00330}.
REGION 241 243 Substrate binding.
{ECO:0000256|PIRSR:PIRSR036687-2}.
REGION 415 417 Substrate binding.
{ECO:0000256|PIRSR:PIRSR036687-2}.
METAL 711 711 Iron-sulfur (4Fe-4S).
{ECO:0000256|PIRSR:PIRSR036687-1}.
METAL 769 769 Iron-sulfur (4Fe-4S).
{ECO:0000256|PIRSR:PIRSR036687-1}.
METAL 772 772 Iron-sulfur (4Fe-4S).
{ECO:0000256|PIRSR:PIRSR036687-1}.
BINDING 198 198 Substrate.
{ECO:0000256|PIRSR:PIRSR036687-2}.
BINDING 499 499 Substrate.
{ECO:0000256|PIRSR:PIRSR036687-2}.
BINDING 791 791 Substrate.
{ECO:0000256|PIRSR:PIRSR036687-2}.
BINDING 796 796 Substrate.
{ECO:0000256|PIRSR:PIRSR036687-2}.
SEQUENCE 857 AA; 94350 MW; F24514B7B3214CF9 CRC64;
MKNLETLLKD YADHVAERAA KGIPPLPLNA EQTNCITKLL EQDSTYDSSY LLDLLINRVP
PGVDEAAYVK ASWLTAIVNS EKYCKSINPE KAIEILGTMI GGYNVNSLVE ILKGEKSLLA
KKAAEVLKNI ILVYDSANEI YELSHSNIYA KEVVNSWANA EWFINKKVLE KEITCLVFKV
DGETNTDDLS PAVHATTRPD IPMHALAMLE FKKPDGLKIL DNLKKQNLPI AYVGDVVGTG
SSRKSAINSL IWHIGEDIAF VPNKKTGGII IGSKIAPIFF NTAQDSGALP IEADVSQMKT
GDVIKIYPYK GIIKKIEKDS NTEELISKFE LYPSTLTDEI QAGGRINLMI GRSLTDKIRN
KLDYQPSEIF TRPQNPTESN AGFTQAQKIV GKACGLEGVR PGMTCEPIMT TVGSQDTTGP
MTRDELKELA CLGFTADLVM QSFCHTAAYP KPVDLVTHKE LPDFISQRGG VALKPGDGII
HSWLNRMLLP DTVGTGGDSH TRFPLGISFP GGSGIVAFAA AIGSMPLNMP ESVLIKFKGE
LLPGITLRDL VNAIPLFAIK KGLLTVEKAN KKNIFNGKIM EIEGLPNLKL EQAFELTDAT
AERSCAGSTI LLSQETVQEY LKSNICLLEK MIESNYEDSK SISRRINDMK NWLKKPSLIQ
PDSNAQYEEI IEIDLAKVTQ PIVACPNDPD NVKEITDVAN TNIDEVFIGS CMTNIGHYRA
AAKVLEGVQN LKAKLWICPP TKMDEETLKA EGYYKIFEDC GARLELPGCS LCMGNQARVD
EGSVVFSTST RNFDNRLGKN AQVFLGSAEL AAVCALLGKI PEVEEYQDIT KNKINPYSDE
LYRYLQFDEI HDFSLTQ


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