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Database: UniProt
Entry: F9RBF4_VIBSN
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Original site: F9RBF4_VIBSN 
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}.
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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
//
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