ID K6YGK2_9ALTE Unreviewed; 866 AA.
AC K6YGK2;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 24-JAN-2024, entry version 39.
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 Name=acnA {ECO:0000313|EMBL:GAC15758.1};
GN ORFNames=GLIP_3137 {ECO:0000313|EMBL:GAC15758.1};
OS Aliiglaciecola lipolytica E3.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Aliiglaciecola.
OX NCBI_TaxID=1127673 {ECO:0000313|EMBL:GAC15758.1, ECO:0000313|Proteomes:UP000006334};
RN [1] {ECO:0000313|EMBL:GAC15758.1, ECO:0000313|Proteomes:UP000006334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=E3 {ECO:0000313|EMBL:GAC15758.1,
RC ECO:0000313|Proteomes:UP000006334};
RX PubMed=25009843;
RA Qin Q.-L., Xie B.-B., Yu Y., Shu Y.-L., Rong J.-C., Zhang Y.-J.,
RA Zhao D.-L., Chen X.-L., Zhang X.-Y., Chen B., Zhou B.-C., Zhang Y.-Z.;
RT "Comparative genomics of the marine bacterial genus Glaciecola reveals the
RT high degree of genomic diversity and genomic characteristic for cold
RT adaptation.";
RL Environ. Microbiol. 16:1642-1653(2014).
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:GAC15758.1}.
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DR EMBL; BAEN01000059; GAC15758.1; -; Genomic_DNA.
DR AlphaFoldDB; K6YGK2; -.
DR STRING; 1127673.GLIP_3137; -.
DR eggNOG; COG1048; Bacteria.
DR Proteomes; UP000006334; 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:GAC15758.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006334}.
FT DOMAIN 66..534
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 666..789
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 866 AA; 95077 MW; 31938DA8EF6977A2 CRC64;
MMNTQYRKRL PNSKLDYFDT REAVDAIKPG AYDTLPYTSR VLAENLVRKC DPEMLNAALE
QIIERKRDLD FPWFPARVVC HDILGQTALV DLAGLRDAIA LKGGDPAKVN PVVPTQLIVD
HSLAVEHAGF ETDAFEKNRA IEDRRNEDRF HFINWTKTAF KNIDVIPPGN GIMHQINLEK
MSPVVHARDG VAFPDTLVGT DSHTPHVDAL GVIALGVGGL EAESVMLGRA SYMRLPNIIG
VELTGKRQPG ITATDIVLSI TEFLRNQRVV SAYLEFYGEG AANLTLGDRA TISNMTPEFG
ASAAMFYIDD KTIDYLKLTG RDEEQVQLVE NYAKHTGLWA DTLNNAQYER VLQFDLSTVG
RNLAGPSNPH RRVSTNDLAA LGISGTVENQ AGLMPDGAVI IAAITSCTNT SNPRNVIAAG
LIARNANKLG LTRKPWVKTS LAPGSKAVQL YLEESNLLPE LEQLGFGIVG FACTTCNGMS
GALDPKIQQE VIERDLYATA VLSGNRNFDG RIHPYAKQAF LASPPLVVAY AIAGTIRFDI
EKDVLGTDPQ GNPITLKDLW PTDEEIDAIV ASSVKPEQFK KVYDPMFDLS VDYGEDIDPL
YDWREKSTYI RRPPYWEGAL AAPRNMKGMR ALAVLGDNIT TDHLSPSNAI MADSAAGEYL
LSMDVPEVDF NSYATHRGDH LTAQRATFAN PKLLNEMVME NGDIKQGSLT RLEPEGKVMR
MWDAIETYMQ RKQPLIIIAG ADYGQGSSRD WAAKGVRLAG VEVIVAEGFE RIHRTNLIGM
GVLPLEFEAG TTRKTLNIDG SEVFDVKGNR QPGASLTLVI HRSNGESLEV PVNCRLDTAE
EASIYEAGGV LQRFAQDFLE SEGQTA
//
