ID A0A0D6PHS6_9PROT Unreviewed; 895 AA.
AC A0A0D6PHS6;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 40.
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=Aam_056_017 {ECO:0000313|EMBL:GAN80753.1};
OS Acidocella aminolytica 101 = DSM 11237.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acidocella.
OX NCBI_TaxID=1120923 {ECO:0000313|EMBL:GAN80753.1, ECO:0000313|Proteomes:UP000032668};
RN [1] {ECO:0000313|EMBL:GAN80753.1, ECO:0000313|Proteomes:UP000032668}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=101 / DSM 11237 {ECO:0000313|Proteomes:UP000032668};
RA Azuma Y., Higashiura N., Hirakawa H., Matsushita K.;
RT "Whole genome sequence of Acidocella aminolytica 101 = DSM 11237.";
RL Submitted (NOV-2012) 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:GAN80753.1}.
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DR EMBL; BANC01000055; GAN80753.1; -; Genomic_DNA.
DR RefSeq; WP_048879146.1; NZ_FQVJ01000013.1.
DR AlphaFoldDB; A0A0D6PHS6; -.
DR STRING; 1120923.SAMN02746095_01830; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR Proteomes; UP000032668; 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:UP000032668}.
FT DOMAIN 74..562
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 693..820
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 895 AA; 97258 MW; 7B5B20932B9D3A54 CRC64;
MTAIGHDSLE TKKTLNVDGK SYEYFSLPAA AAKLGDISKL PKTLKILLEN VLRFENGGSY
TTEDAKSIIA WLEKANSSKE VPFKPARILM QDFTGVPAVV DLAAMRDGIV KLGAEPEKVN
PLIPVDLVID HSVMVDYSAS HDALQKNIDL EFERNSERYR FLRWGQEAFN NFRVVPPGTG
ICHQVNLEYL AQVAWTSENG GKTYVYPDTL YGTDSHTTMV NGLGVLGWGV GGIEAEAAML
GQPIAMLIPD VVGFKLTGKL SEGVTATDLV LTVTQMLRAK KVVGKFVEFY GEGMAEMALA
DRATIANMAP EYGATCGFFP VDEVTLDYLR LSGRDEHRIK LVEEYTKTQG LWRDEHEPVF
SDTLELDLST VQPSLAGPKR PQDRVLLKEA ASAFKSELTK SLGVPAEAVA NKGAVAGTNY
EITHGDVVIA AITSCTNTSN PYVLVAAGLV ARKARELGLA PKPWVKTSLA PGSQVVTDYL
NKSGLTEDLD AIGFETVGYG CTTCIGNSGP LPDPIVDAIE NNKLVAVSVL SGNRNFEGRV
HPNVRANYLA SPPLVVAYSL FGNMREDITT AQIGTSKDGK PVYLKDIWPS NKEIQDIVGQ
VLTREMFQAR YSDVFKGPAE WQAIEFSGGT DTYAWPAGST YVKNPPYFQD ITPEPKAVSD
IKGARVMALL GDSITTDHIS PAGNIKKSSP AGVFLSEHQV QQKDFNSYGS RRGNDDVMVR
GTFANIRIKN EMMGGTEGGN TKHYPGGEEM SIYDAAMKYK QEGVPLVVFA GQEYGTGSSR
DWAAKGTMLL GVKAVIAESF ERIHRSNLVG MGVLPLLFKN GETRKSLGLT GEETVDIVGL
ENLSPRMDIK AIITRPDGSK KEIELLCRVD TADEVNYYKH GGILQYVLRG MAKAA
//
