ID A0A1F1Q848_9PSED Unreviewed; 913 AA.
AC A0A1F1Q848;
DT 15-FEB-2017, integrated into UniProtKB/TrEMBL.
DT 15-FEB-2017, sequence version 1.
DT 27-MAR-2024, entry version 30.
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 ORFNames=HMPREF3173_12330 {ECO:0000313|EMBL:OFS73286.1};
OS Pseudomonas sp. HMSC08G10.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1581141 {ECO:0000313|EMBL:OFS73286.1, ECO:0000313|Proteomes:UP000179079};
RN [1] {ECO:0000313|EMBL:OFS73286.1, ECO:0000313|Proteomes:UP000179079}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HMSC08G10 {ECO:0000313|EMBL:OFS73286.1,
RC ECO:0000313|Proteomes:UP000179079};
RA Evans L.H., Alamgir A., Owens N., Weber N.D., Virtaneva K., Barbian K.,
RA Babar A., Rosenke K.;
RL Submitted (APR-2016) 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}.
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:OFS73286.1}.
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DR EMBL; LWMZ01000049; OFS73286.1; -; Genomic_DNA.
DR RefSeq; WP_070573388.1; NZ_KV793306.1.
DR AlphaFoldDB; A0A1F1Q848; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000179079; 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}.
FT DOMAIN 76..581
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 710..836
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 413..436
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 913 AA; 99120 MW; 368C72474EFF9398 CRC64;
MPSLDSLKTL KTLKVADRTY HYFSLAEAAR QLGDLQRLPM SLKVLLENLL RWEDGKTVTG
DDLRALAGWL GERHSDREIQ YRPARVLMQD FTGVPAVVDL AAMRAAMAKA GGDPQRINPL
SPVDLVIDHS VMVDRYASPA AFAQNVDIEM QRNGERYAFL RWGQSAFDNF RVVPPGTGIC
HQVNLEYLGR TVWTREADGR IYAFPDTLVG TDSHTTMING LGVLGWGVGG IEAEAAMLGQ
PVSMLIPEVI GFKLTGKLRE GITATDLVLT VTQMLRKKGV VGKFVEFYGD GLADLPLADR
ATIANMAPEY GATCGFFPVD QVTLDYLRLS GRPEEAVQLV EAYCKAQGLW RVPGHEPAFS
DTLSLDMHDV EASLAGPKRP QDRVALSQVS QAFEGFIELQ PKPLAKEVGR LESEGGGGVA
VGNADQTGEI DYTHDGQTHT LRDGAVVIAA ITSCTNTSNP SVMMAAGLVA KKAVEKGLTR
KPWVKSSLAP GSKVVTDYFK AAGLTPYLDQ LGFALVGYGC TTCIGNSGPL DDAIEQAIGS
ADLTVASVLS GNRNFEGRVH PLVKTNWLAS PPLVVAYALA GSVRTDLTRD PLGIGKDGQP
VFLRDIWPSQ QEIAEAVAKV DTAMFHKEYA EVFAGDAQWQ AIEVPQAATY VWQDDSTYIQ
HPPFFDTIGG PLPQVRDIQG ARILALLGDS VTTDHISPAG NIKAESPAGR YLRSKGVEPR
DFNSYGSRRG NHEVMMRGTF ANIRIRNEML AGEEGGNTLH VPSGEKLSIY DAAMRYQDEG
TPLVVIAGQE YGTGSSRDWA AKGTNLLGVK AVLAESFERI HRSNLVGMGV LPLQFRAGEN
RKTLGLTGKE RIDVQGLTDA QLRPGMTLAL RITREDGQQQ QTEVLCRIDT LNEVEYFKSG
GILHYVLRQL IAA
//
