ID D7WCQ2_9CORY Unreviewed; 926 AA.
AC D7WCQ2;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 67.
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:EFK53933.1};
GN ORFNames=HMPREF0291_11590 {ECO:0000313|EMBL:EFK53933.1};
OS Corynebacterium genitalium ATCC 33030.
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales;
OC Corynebacteriaceae; Corynebacterium.
OX NCBI_TaxID=585529 {ECO:0000313|EMBL:EFK53933.1, ECO:0000313|Proteomes:UP000004208};
RN [1] {ECO:0000313|EMBL:EFK53933.1, ECO:0000313|Proteomes:UP000004208}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 33030 {ECO:0000313|EMBL:EFK53933.1,
RC ECO:0000313|Proteomes:UP000004208};
RA Muzny D., Qin X., Buhay C., Dugan-Rocha S., Ding Y., Chen G., Hawes A.,
RA Holder M., Jhangiani S., Johnson A., Khan Z., Li Z., Liu W., Liu X.,
RA Perez L., Shen H., Wang Q., Watt J., Xi L., Xin Y., Zhou J., Deng J.,
RA Jiang H., Liu Y., Qu J., Song X.-Z., Zhang L., Villasana D., Johnson A.,
RA Liu J., Liyanage D., Lorensuhewa L., Robinson T., Song A., Song B.-B.,
RA Dinh H., Thornton R., Coyle M., Francisco L., Jackson L., Javaid M.,
RA Korchina V., Kovar C., Mata R., Mathew T., Ngo R., Nguyen L., Nguyen N.,
RA Okwuonu G., Ongeri F., Pham C., Simmons D., Wilczek-Boney K., Hale W.,
RA Jakkamsetti A., Pham P., Ruth R., San Lucas F., Warren J., Zhang J.,
RA Zhao Z., Zhou C., Zhu D., Lee S., Bess C., Blankenburg K., Forbes L.,
RA Fu Q., Gubbala S., Hirani K., Jayaseelan J.C., Lara F., Munidasa M.,
RA Palculict T., Patil S., Pu L.-L., Saada N., Tang L., Weissenberger G.,
RA Zhu Y., Hemphill L., Shang Y., Youmans B., Ayvaz T., Ross M.,
RA Santibanez J., Aqrawi P., Gross S., Joshi V., Fowler G., Nazareth L.,
RA Reid J., Worley K., Petrosino J., Highlander S., Gibbs R.;
RL Submitted (JUN-2010) 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=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate = 2-methyl-cis-
CC aconitate + H2O; Xref=Rhea:RHEA:17941, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:57429, ChEBI:CHEBI:57872; EC=4.2.1.99;
CC Evidence={ECO:0000256|ARBA:ARBA00000118};
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 -!- PATHWAY: Organic acid metabolism; propanoate degradation.
CC {ECO:0000256|ARBA:ARBA00005026}.
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:EFK53933.1}.
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DR EMBL; ACLJ02000003; EFK53933.1; -; Genomic_DNA.
DR RefSeq; WP_005290103.1; NZ_CP072935.1.
DR AlphaFoldDB; D7WCQ2; -.
DR STRING; 585529.HMPREF0291_11590; -.
DR eggNOG; COG1048; Bacteria.
DR HOGENOM; CLU_013476_2_1_11; -.
DR OrthoDB; 9764318at2; -.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000004208; Chromosome.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
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.
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:EFK53933.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000004208}.
FT DOMAIN 73..590
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 719..848
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 926 AA; 101106 MW; E498ABD47693DD26 CRC64;
MSESKNSFNA KKTLEVGGKS YDYYALDAVE GMEKLPYSLK VLGENLLRTE DGKNVTEEHI
NAIANWDPSA EPSIEIQFTP ARVLMQDFTG VPCVVDLATM REAVSSLGGN PDQVNPLNPA
EMVIDHSVII EAFGSESAID KNVEIEYERN EERYQFLRWG AENFSNFRVV PPGTGIVHQV
NIEYLSRVVF DNDGVAYPDT CIGTDSHTTM ENGLGILGWG VGGIEAEAAM LGQPVSMLIP
RVVGFKLTGE IPVGVTATDV VLTVTEMLRE HGVVQKFVEF YGNGVKEIPL ANRATIGNMS
PEFGSTCAIF PIDEETINYL ELTGRDKETI DRVEAYAKAQ GMWLEQDAPE AEYSEYLELD
LSTVKPSIAG PKRPQDRILL EESKTTFRTQ LPDYNTAGEG QAEPVRAEKV DTVEYNQSWP
ANGESAAEGA EGRASKPVIV ESPQGGEYTL DHGMVAIAAI TSCTNTSNPS VMVGAAMLAR
KAAEKGLKAK PWVKTIMAPG SQVVNGYYER ADLWKDLEAV GFYLSGFGCA SCIGNSGPLP
NEISEAINEY DLTATAVLSG NRNFEGRISP DVKMNYLASP LLVIAYAIAG TMDFDFESQP
LGQDADGNDI FLKDVWPSPE EIEGVIAETI SREMYEADYA DVFKGDEQWQ NLDVPEGKTF
AWDEDSTYIR KAPYFDGMPE EPNDVGDITG ARVLAKLGDS VTTDHISPAS SIKPGTPAAN
YLDDNGVERH DYNSFGSRRG NHEVMVRGTF ANIRLRNQLV EDAGGYTLDF TQEGNPQAFI
YDAAQNYAEH DIPLVVLAGK EYGTGSSRDW AAKGTNLLGV KAVITESFER IHRSNLIGMG
VLPLQFPEGE SHESLGLDGT ETFDITGITA FNEGDTIPET VHVTATKDGG ETVEFDAKVR
VDTPGEAEYY RHGGILQYVL RQMVKS
//
