ID A0A0C5W404_9GAMM Unreviewed; 861 AA.
AC A0A0C5W404;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=Aconitate hydratase {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926, ECO:0000256|RuleBase:RU361275};
GN ORFNames=H744_1c1146 {ECO:0000313|EMBL:AJR06171.1};
OS Photobacterium gaetbulicola Gung47.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Photobacterium.
OX NCBI_TaxID=658445 {ECO:0000313|EMBL:AJR06171.1, ECO:0000313|Proteomes:UP000032303};
RN [1] {ECO:0000313|EMBL:AJR06171.1, ECO:0000313|Proteomes:UP000032303}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Gung47 {ECO:0000313|EMBL:AJR06171.1,
RC ECO:0000313|Proteomes:UP000032303};
RA Kim Y.-O.;
RT "Complete genome sequence of the lipase-producing bacterium Photobacterium
RT gaetbulicola Gung47.";
RL Submitted (MAY-2013) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the isomerization of citrate to isocitrate via cis-
CC aconitate. {ECO:0000256|RuleBase:RU361275}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=citrate = D-threo-isocitrate; Xref=Rhea:RHEA:10336,
CC ChEBI:CHEBI:15562, ChEBI:CHEBI:16947; EC=4.2.1.3;
CC Evidence={ECO:0000256|ARBA:ARBA00023501,
CC ECO:0000256|RuleBase:RU361275};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; CP005973; AJR06171.1; -; Genomic_DNA.
DR RefSeq; WP_044621334.1; NZ_CP005973.1.
DR AlphaFoldDB; A0A0C5W404; -.
DR STRING; 658445.H744_1c1146; -.
DR KEGG; pgb:H744_1c1146; -.
DR PATRIC; fig|658445.3.peg.1236; -.
DR HOGENOM; CLU_013476_2_1_6; -.
DR OrthoDB; 9764318at2; -.
DR Proteomes; UP000032303; Chromosome 1.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0019679; P:propionate metabolic process, methylcitrate cycle; IEA:InterPro.
DR Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
DR InterPro; IPR012708; 2Me_IsoCit_deHydtase_FeS-dep.
DR InterPro; IPR015931; Acnase/IPM_dHydase_lsu_aba_1/3.
DR InterPro; IPR001030; Acoase/IPM_deHydtase_lsu_aba.
DR InterPro; IPR015928; Aconitase/3IPM_dehydase_swvl.
DR InterPro; IPR006249; Aconitase/IRP2.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR02333; 2met_isocit_dHY; 1.
DR NCBIfam; TIGR01341; aconitase_1; 1.
DR PANTHER; PTHR11670:SF43; 2-METHYLCITRATE DEHYDRATASE (2-METHYL-TRANS-ACONITATE FORMING); 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR Pfam; PF00330; Aconitase; 1.
DR Pfam; PF00694; Aconitase_C; 1.
DR PRINTS; PR00415; ACONITASE.
DR SUPFAM; SSF53732; Aconitase iron-sulfur domain; 1.
DR SUPFAM; SSF52016; LeuD/IlvD-like; 1.
PE 3: Inferred from homology;
KW 4Fe-4S {ECO:0000256|RuleBase:RU361275};
KW Iron {ECO:0000256|ARBA:ARBA00023004, ECO:0000256|RuleBase:RU361275};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014, ECO:0000256|RuleBase:RU361275};
KW Lyase {ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000032303}.
FT DOMAIN 68..535
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 658..789
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 861 AA; 94756 MW; 484905E1210D2C60 CRC64;
MKMNTRYRKP LADTGLDFFD TREAVNEISP DAYETLPYTS RVLAEQLIRR CDPESLAASL
KQIIDRKRDL DFPWYPARVV CHDILGQTAL VDLAGLRDAI AEQGGDPSKV NPVVETQLIV
DHSLAVEYAG FDPDAFDKNR AIEERRNEDR FHFIEWCKTA FENVSVIPAG NGIMHQINLE
KMSPVVQTKN GVAYPDTCVG TDSHTPHVDA LGVIAIGVGG LEAETVMLGR PSMMRLPDIV
GVNLTGKRQP GITATDIVLA ITEFLRNERV VSSYLEFFGE GARDLTIGDR ATISNMTPEY
GATAGMFYID EQTINYLKLT GRDEQQVELV EKYAKQAGLW ADDLKHAEYE RVLEFDLSTV
SRNMAGPSNP HRRLPTSELA ARGISGDWNE TEGELPDGAV IIAAITSCTN TSNPRNVVAA
GLLAKKANEL GLVRKPWVKS SFAPGSKVAK LYLQDAGLLP ELEKLGFGIV AYACTTCNGM
SGALDPKIQQ EIIDRDLYTT AVLSGNRNFD GRIHPYAKQA FLASPPLVVA YALAGTIRFD
IERDSLGTDS QGKPVYLNDL WPSDEEIDAV VGQYVKPEQF NQVYIQMFKL DDEQRNSNPL
YDWRPMSTYI RRPPYWEGAL AGERTLSGMR PLALLGDNIT TDHLSPSNAI LASSAAGEYL
AKMGLPEEDF NSYATHRGDH LTAQRATFAN PKLFNEMVKQ DGEVVQGSLA RIEPEGKVVR
MWEAIETYMN RKQPLIVVAG ADYGQGSSRD WAAKGVRLAG VEAIVAEGFE RIHRTNLVGM
GVLPLQFKEG INRNTLALDG TELYDVVGEI QPGADLALVV TRTNGEKVDV PVTCRLDTAD
EVAVYAAGGV LQRFAKDFLA Q
//
