ID A0A0L9V5Q0_PHAAN Unreviewed; 1475 AA.
AC A0A0L9V5Q0;
DT 11-NOV-2015, integrated into UniProtKB/TrEMBL.
DT 11-NOV-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE RecName: Full=aconitate hydratase {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
GN ORFNames=LR48_Vigan08g119800 {ECO:0000313|EMBL:KOM50371.1};
OS Phaseolus angularis (Azuki bean) (Vigna angularis).
OC Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Vigna.
OX NCBI_TaxID=3914 {ECO:0000313|EMBL:KOM50371.1, ECO:0000313|Proteomes:UP000053144};
RN [1] {ECO:0000313|Proteomes:UP000053144}
RP NUCLEOTIDE SEQUENCE.
RC STRAIN=cv. Jingnong 6 {ECO:0000313|Proteomes:UP000053144};
RX PubMed=26460024; DOI=10.1073/pnas.1420949112;
RA Yang K., Tian Z., Chen C., Luo L., Zhao B., Wang Z., Yu L., Li Y., Sun Y.,
RA Li W., Chen Y., Li Y., Zhang Y., Ai D., Zhao J., Shang C., Ma Y., Wu B.,
RA Wang M., Gao L., Sun D., Zhang P., Guo F., Wang W., Li Y., Wang J.,
RA Varshney R.K., Wang J., Ling H.Q., Wan P.;
RT "Genome sequencing of adzuki bean (Vigna angularis) provides insight into
RT high starch and low fat accumulation and domestication.";
RL Proc. Natl. Acad. Sci. U.S.A. 112:13213-13218(2015).
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; CM003378; KOM50371.1; -; Genomic_DNA.
DR STRING; 3914.A0A0L9V5Q0; -.
DR EnsemblPlants; KOM50371; KOM50371; LR48_Vigan08g119800.
DR Gramene; KOM50371; KOM50371; LR48_Vigan08g119800.
DR OMA; PCHASEC; -.
DR Proteomes; UP000053144; Chromosome 8.
DR GO; GO:0016836; F:hydro-lyase activity; IEA:UniProt.
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:0043436; P:oxoacid metabolic process; IEA:UniProt.
DR CDD; cd01586; AcnA_IRP; 1.
DR CDD; cd01580; AcnA_IRP_Swivel; 1.
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; IPR044137; AcnA_IRP_Swivel.
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; IPR018136; Aconitase_4Fe-4S_BS.
DR InterPro; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01341; aconitase_1; 1.
DR PANTHER; PTHR11670; ACONITASE/IRON-RESPONSIVE ELEMENT FAMILY MEMBER; 1.
DR PANTHER; PTHR11670:SF54; CYTOPLASMIC ACONITATE HYDRATASE; 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.
DR PROSITE; PS00450; ACONITASE_1; 1.
DR PROSITE; PS01244; ACONITASE_2; 1.
PE 3: Inferred from homology;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000053144}.
FT DOMAIN 604..1106
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 1274..1401
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 1475 AA; 161566 MW; AF37F924CF078CF2 CRC64;
MPSLPLATGA SSLGERPLLR PRWTSVLAGR RASSRWASIY LLITGERSLD ERPQLAGRAS
SLGERVSSRW ASVHLLVSLD ERPFAGRTFV LAGRASVLAE RTSSASSASC ARQYVFGLNG
SVIRPQRFSP FGLNLSAIRP HEYSVIRPHV FAIRPQPLGH SASTIRPSGL NCSVIQPQAL
GHSASSSRPS GLNLSVIRPQ PFGPPASTVR PFSLKLSAIR PHLLAKFGLN NSAIRPHRYM
FALTSFHHST SLVFGHSASG MYLASTSRPF DLNLSPIRPQ PLGHSASTSR PFGLTSIRPE
VLRQIWHQVF DLNLLVKFGL NNSAIRPQRY VFGINVSAIR PHRFSSFGLN FSAIRPNKCS
AIRPQALCHP ASTIRLFSLN CSAIRPKLIE EAGEVSLDEG AVLTSESIVT IIIVLINFNF
NFNFNFTLLQ AYRSRTFFSF PNHPCHASEC VIITMYITTS SSSSSSLLGA TTPKLLSSSP
SRTFAFPPSF TPYSSRNPLR SSLPRWSHRL HHVSPLTLRP PIRAVAPAVE RFHREIANAA
NENPFKGNLT SLPKPGGGEF GKFYSLPSLN DPRIDRLPYS IRILLESAIR NCDNFQVKKE
DVEKILAWEI NSTKQVEIPF KPARVLLQDF TGVPVVVDLA CMRDAMNKLG SDSNKINPLV
PVDLVIDHSV QVDVTRSENA VQANMELEFQ RNKERFAFLK WGSTAFRNML VVPPGSGIVH
QVNLEYLGRV VFNNEGLLYP DSVVGTDSHT TMIDGLGVAG WGVGGIEAEA AMLGQPMSMV
LPGVVGFKLY GKLGNGVTAT DLVLTVTQIL RKHGVVGKFV EFYGDGMGEL SLADRATIAN
MSPEYGATMG FFPVDHVTLQ YLKLTGRSDD NVAMIESYLR ANKLFVDYNE PQQDRVYTSH
LELNLSEVEP CISGPKRPHD RVPLKEMKAD WHACLDNKVG FKGFAIPKEA QGNVAKFDFH
GQPAELKHGS VVIAAITSCT NTSNPSVMLG AGLVAKKARE LGLQVKPWVK TSLAPGSGVV
TKYLHQSGLQ KYLNEQGFHI VGFGCTTCIG NSGELDESVS SAISENDIVA AAVLSGNRNF
EGRVHPLTRA NYLASPPLVV AYALAGTVDI DFEKEPIGTG ENGKNVYLRD IWPSTEEIAE
TRNFNRNSGH QKAILVRKLQ ENISQLLSNP ACCLTCSEAH TRLLPKGILX XXXXXXXXXX
XXXWNHLQVT ADSLYSWDLN STYIHEPPYF KNMTMDPPGP HGVKDAYCLL NFGDSITTDH
ISPAGSIHKD SPAAKYLLER GVEPKDFNSY GSRRGNDEVM ARGTFANIRL VNKLLNGDVG
PKTIHVPTGE KLYVFEAATR YMASGQDTIV VAGAEYGSGS SRDWAAKGPM LLGVKAVIAK
SFERIHRSNL VGMGIIPLCF KSGEDADTLG LTGHERYTID LPSTIIEIRP GQDVTVTTDN
GKSFTCTIRF DTEVELAYFN HGGILPYVIR NLIKE
//
