ID F9RBF4_VIBSN Unreviewed; 867 AA.
AC F9RBF4;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
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=VIBRN418_06421 {ECO:0000313|EMBL:EGU34401.1};
OS Vibrio sp. (strain N418).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=701176 {ECO:0000313|EMBL:EGU34401.1, ECO:0000313|Proteomes:UP000003627};
RN [1] {ECO:0000313|EMBL:EGU34401.1, ECO:0000313|Proteomes:UP000003627}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=N418 {ECO:0000313|EMBL:EGU34401.1,
RC ECO:0000313|Proteomes:UP000003627};
RA Strain E.A., Brown E., Allard M.W.;
RL Submitted (AUG-2011) 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}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGU34401.1}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AFWD01000045; EGU34401.1; -; Genomic_DNA.
DR RefSeq; WP_009733762.1; NZ_AFWD01000045.1.
DR AlphaFoldDB; F9RBF4; -.
DR eggNOG; COG1048; Bacteria.
DR OMA; GRASYMR; -.
DR Proteomes; UP000003627; Unassembled WGS sequence.
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; 6.10.190.10; -; 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; 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, ECO:0000313|EMBL:EGU34401.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723}.
FT DOMAIN 66..541
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 664..795
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 867 AA; 95132 MW; 8E8A1BF8C4AE84DC CRC64;
MSINSQYRKP LIGTELEYFD ARAAVDAIAE NAYQSLPYTS RVFAEQLVRR CDPAMLDASL
KQLIERKRDL DFPWYPARVV CHDILGQTAL VDLAGLRDAI AEQGGDPAKV NPVVETQLIV
DHSLAVEHAG FDREAFDKNR AIEDRRNQDR FDFIEWCKTA FENVSVIPAG NGIMHQINLE
KMSPVVQVKQ GVAYPDTCVG TDSHTPHVDA LGVIAIGVGG LEAETVMLGR PSMMRLPDIV
GVNITGQRQA GITATDIVLA MTEFLRNERV VSCYLEFFGE GARALTIGDR ATISNMTPEY
GATAGMFYID EQTIHYLKLT GRDDEQIALV ENYAKQTGLW ADDLQNAEYE RVLEFDLSSV
TRNMAGPSNP HSRLPTSELA ARGIADGAKL NADKLGADQN LPDGAVIIAA ITSCTNTSNP
RNVVAAALVA KKANQLGLTR KPWVKTSFAP GSKVAKLYLE EAGLLTELEQ LGFGIVGYAC
TTCNGMSGAL EPAIQQEIIE RDLYTTAVLS GNRNFDGRIH PYAKQAFLAS PPLVVAYALA
GTMRFDIERD ALGINSQGES IYLSDLWPSD QEIDAVVKTS VKPEQFKQVY IQMFKLDNDR
QTTKPLYDWR EMSTYIRRPP YWQGALAGER TLSAMRPLAI LGDNITTDHL SPSNAILPTS
AAGEYLAQMG LPEEDFNSYA THRGDHLTAQ RATFANPKLF NEMVKDNGEV VQGSLARVEP
EGQVMRMWEA IETYMQRKQP LIVIAGADYG QGSSRDWAAK GVRLAGVEVI VAEGFERIHR
TNLVGMGVLP LQFKAGTNRH TLALDGSELY DVVGEISAGV DLALVITRTN GDKLDVAVTC
RLDTADELHV YQAGGVLQRF AQDFLAE
//