ID C9P4W7_VIBME Unreviewed; 865 AA.
AC C9P4W7;
DT 24-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 24-NOV-2009, sequence version 1.
DT 24-JAN-2024, entry version 50.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=VIB_001337 {ECO:0000313|EMBL:EEX37221.1};
OS Vibrio metschnikovii CIP 69.14.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=675813 {ECO:0000313|EMBL:EEX37221.1, ECO:0000313|Proteomes:UP000005604};
RN [1] {ECO:0000313|EMBL:EEX37221.1, ECO:0000313|Proteomes:UP000005604}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CIP 69.14 {ECO:0000313|EMBL:EEX37221.1,
RC ECO:0000313|Proteomes:UP000005604};
RG Los Alamos National Laboratory (LANL);
RG National Microbial Pathogen Data Resource (NMPDR);
RA Munk A.C., Tapia R., Green L., Rogers Y., Detter J.C., Bruce D.,
RA Brettin T.S., Colwell R.R., Huq A., Grim C.J., Hasan N.A., Bartels D.,
RA Vonstein V.;
RL Submitted (OCT-2009) to the EMBL/GenBank/DDBJ databases.
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 -!- 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}.
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DR EMBL; ACZO01000006; EEX37221.1; -; Genomic_DNA.
DR RefSeq; WP_004395320.1; NZ_ACZO01000006.1.
DR AlphaFoldDB; C9P4W7; -.
DR STRING; 675813.VIB_001337; -.
DR GeneID; 79887719; -.
DR eggNOG; COG1048; Bacteria.
DR Proteomes; UP000005604; Unassembled WGS sequence.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
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; 6.10.190.10; -; 1.
DR Gene3D; 3.40.1060.10; Aconitase, Domain 2; 1.
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; IPR015932; Aconitase_dom2.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR02333; 2met_isocit_dHY; 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:EEX37221.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000005604}.
FT DOMAIN 66..535
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 658..788
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 865 AA; 95087 MW; 75FF448D4551EDA9 CRC64;
MKSRFRQTLP GTEINYFDAR AAINAIKPDA YQRLPYTSRI LAENLVRCCP GEQLTSALTQ
LIERKQDRDF PWYPARVVCH DILGQTALVD LAGLRDAIAE QGGDPAQVNP IVETQLIVDH
SLAVEHAGFD ADALVKNRAI EDRRNEDRFH FIEWCKHAFK NVSVIPAGNG IMHQINLEKM
SPVIQLKQGV AFPDTCVGTD SHTPHINALG VIAIGVGGLE AETVMLGRPS MMRLPDIVGV
KLIGQRQAGI TATDIVLALT EFLRTQRVVS AYLEFFGEGA HQLTIGDRAT IANMTPEYGA
SAGLFYIDQQ TLRYLQLTGR EPDQIALVEQ YAKQTGLWAD ALLEVQYERV LTFDLSQVER
TMAGPSQPHR CLPTSQLVER GIADTLRQES TQFGLPDGAV IIAAITSCTN TSNPRNLVAA
GLLAKKANQR GLIRQPWVKS SFAPGSKVAK LYLEEANLLT ELETLGFGIV GYACTTCNGM
SGALDPAIER EILARDLYTT AVLSGNRNFD GRIHPHAKHA FLASPPLVVA YAIAGSIRFD
IERDALGVDS QGTPIYLADI WPSDEEIDAV VESCVKPQQY QHVYIQMFQL QDSTQQASPL
YDWRPHSTYI RRPPYWQGAL AGKPSLTAMR PLAILGDNVT TDHLSPSNAI LASSAAGEYL
ASMGVPEADF NSYATHRGDH LTAQRATLAN PKLLNEMVKE NGEVIQGSLA RIEPEGRVTR
LWEAIETYLE RKQPLIIIAG ADYGQGSSRD WAAKGVRLAG VEAIVAEGFE RIHRTNLVGM
GVLPLQFMTG MNRLTLDLDG SELFDVRGVI QPNAILTLTI TRRDQSSFSV SVICRLETED
ELDVYQAGGV LPRFAEQFLT KEKPL
//
