ID A0A095VNP6_9GAMM Unreviewed; 917 AA.
AC A0A095VNP6;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 42.
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=HRUBRA_02438 {ECO:0000313|EMBL:KGE03000.1};
OS Pseudohaliea rubra DSM 19751.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Cellvibrionales; Halieaceae;
OC Pseudohaliea.
OX NCBI_TaxID=1265313 {ECO:0000313|EMBL:KGE03000.1, ECO:0000313|Proteomes:UP000029640};
RN [1] {ECO:0000313|EMBL:KGE03000.1, ECO:0000313|Proteomes:UP000029640}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19751 {ECO:0000313|EMBL:KGE03000.1,
RC ECO:0000313|Proteomes:UP000029640};
RX PubMed=25414506;
RA Spring S., Fiebig A., Riedel T., Goker M., Klenk H.P.;
RT "Genome Sequence of Gammaproteobacterial Pseudohaliea rubra Type Strain DSM
RT 19751, Isolated from Coastal Seawater of the Mediterranean Sea.";
RL Genome Announc. 2:e01208-14(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 -!- 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:KGE03000.1}.
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DR EMBL; AUVB01000077; KGE03000.1; -; Genomic_DNA.
DR RefSeq; WP_035515966.1; NZ_KN234759.1.
DR AlphaFoldDB; A0A095VNP6; -.
DR STRING; 1265313.HRUBRA_02438; -.
DR PATRIC; fig|1265313.6.peg.2406; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_6; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000029640; 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:UP000029640}.
FT DOMAIN 78..586
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 715..842
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 917 AA; 98744 MW; 39E95D018EEFC675 CRC64;
MTHSSAKNSL NTLTDLQVGH RSYGYHSLPR AAKQLGDLER LPFSLKVLLE NLLRYEDDET
VSRSHFDAMA AWLDDKRSKT EIQFRPARVL MQDFTGVPAI VDLAAMRDAL AAAGGDPAKI
NPISPVDLVI DHSVMVDEYG SASAFADNVS IEMQRNQERY EFLRWGQQAF NNFRVVPPGT
GICHQVNLEY LARTVWSDDR HGNLTAFPDT LVGTDSHTTM INGLGVLGWG VGGIEAEAAM
LGQPVSMLIP EVVGFRMNGR LREGITATDL VLTVTEMLRA HGVVGKFVEF FGDGLAQMPV
ADRATIANMA PEYGATCGFF PVDEQTLAYL ELTGRDADQV ALVEAYCKAQ GLWRTPGHEP
SYTSVLELDL DTVEASLAGP KRPQDRVGLS KVRSTFELLM EQGEGTAPAD TGRLESEGGQ
GAVGIDASYL HASSQYCELD GEPLHLNPGA VVIAAITSCT NTSNPSVMMA AGLLAQKAVA
RGLTVKPWVK TSLAPGSRVV TEYLAASGLQ AALDRLGFNL VGYGCTTCIG NSGPLREPIE
KAIVTGDLTV SSVLSGNRNF EGRVHPLVKA NWLASPPLVV AYALAGNVRL DLSRDPIAED
ANGNAVYLAD LWPSQAEVAE AVARVSTAMF RDEYASVFDG DATWQAIKVP DSKTYQWTDS
STYIQHPPYF QGMAPEPGAL TDVEGARILA LLGDSVTTDH ISPAGAFSTD SPAGRYLIEH
GIHKPDFNSY GSRRGNHEVM MRGTFANVRI NNEMLDDVEG GYTRHVPSGE QLSIYDAAMR
YGKEGTPLVV VAGREYGTGS SRDWAAKGTL LLGVRAVIAE SFERIHRSNL IGMGVLPLQF
ADGENRRTLA LTGEETLALH GIAGGVTPGQ TVTLDVTYPD GSTRSCKLKA RIDTANEASY
YAGGGILHYV LRQLMAD
//
