ID A0A1X6YH36_9RHOB Unreviewed; 917 AA.
AC A0A1X6YH36;
DT 05-JUL-2017, integrated into UniProtKB/TrEMBL.
DT 05-JUL-2017, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE RecName: Full=Aconitate hydratase {ECO:0000256|RuleBase:RU361275};
DE Short=Aconitase {ECO:0000256|RuleBase:RU361275};
DE EC=4.2.1.3 {ECO:0000256|RuleBase:RU361275};
GN Name=acnA {ECO:0000313|EMBL:SLN21156.1};
GN ORFNames=ROH8110_00747 {ECO:0000313|EMBL:SLN21156.1};
OS Roseovarius halotolerans.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=505353 {ECO:0000313|EMBL:SLN21156.1, ECO:0000313|Proteomes:UP000193207};
RN [1] {ECO:0000313|EMBL:SLN21156.1, ECO:0000313|Proteomes:UP000193207}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CECT 8110 {ECO:0000313|EMBL:SLN21156.1,
RC ECO:0000313|Proteomes:UP000193207};
RA Afonso C.L., Miller P.J., Scott M.A., Spackman E., Goraichik I.,
RA Dimitrov K.M., Suarez D.L., Swayne D.E.;
RL Submitted (MAR-2017) 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 -!- PATHWAY: Carbohydrate metabolism; tricarboxylic acid cycle; isocitrate
CC from oxaloacetate: step 2/2. {ECO:0000256|ARBA:ARBA00004717}.
CC -!- SIMILARITY: Belongs to the aconitase/IPM isomerase family.
CC {ECO:0000256|ARBA:ARBA00007185, ECO:0000256|RuleBase:RU361275}.
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DR EMBL; FWFU01000001; SLN21156.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1X6YH36; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000193207; 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:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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 4Fe-4S {ECO:0000256|ARBA:ARBA00022485, 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|ARBA:ARBA00023239, ECO:0000256|RuleBase:RU361275};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000193207}.
FT DOMAIN 81..584
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 714..839
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 917 AA; 99752 MW; 2D96B69728A8C4ED CRC64;
MPITVGHDTA KTRKTLSVNG KSYAYYSIKA AEQAGLGDFS RLPAALRVVL ENMLRFEDGK
TVTTDDIKAF SDWADNGGKG NRELAYRPAR VLMQDFTGVP AVVDLAAMRD GIKALGGDPQ
QINPLNPVDL VIDHSVMIDE FGNPRAFQMN VDREYERNME RYQFLKWGQG AFNNFRVVPP
GTGICHQVNL EYLAQTVWTD KDQNGDEVAY PDTLVGTDSH TTMVNGAAVL GWGVGGIEAE
AAMLGQPISM LIPEVVGFEL TGAMIEGTTG TDLVLKVVEM LRKKGVVGKF VEFYGDGLDN
LPLADRATIA NMAPEYGATC GFFPIDDETL RYLRNTGRDE DRLALVEAYA KENGFWRDAS
YAPVYTDTLS LDMGTIVPAI SGPKRPQDYV ALDQAASNFF DVVADYRGED EGRAANDMAA
EGPAPDAMID PRKTAEVEGE DYTLRDGSVV IASITSCTNT SNPYVMIGAG LVARKARELG
LNRKPWVKTS LAPGSQVVSH YLEAAGLQED LDAIGFNLVG YGCTTCIGNS GPLQEEISKA
VNDNDLIATS VLSGNRNFEG RISPDVRANY LASPPLVVVY AIAGDMNIDL TNDPIGTDKD
GKDVYMKDIW PTQAEIAELV ERTVTREAFQ SKYADVFKGD DKWQSVETSD AETYDWPPQS
TYVQNPPYFQ GMSKEAGTIS DIKGARILAL LGDMVTTDHI SPAGSFKPST PAGEYLTERQ
VPVREFNSYG SRRGNHEVMM RGTFANIRIR NEMLDGVEGG YTLGPDGEQT SIFDAAMAWQ
EQDVPLVIVA GEQYGAGSSR DWAAKGTSLL GVKAVIAESY ERIHRSNLVG MGVVPFEFTG
GDTRKTLGLK GDESFDITGL EGDMKPQAEI PCTITYGDGT TKEITLKSRI DTAVEKEYVE
NGGVLHYVLR NLARSAA
//
