ID K5BG91_MYCHD Unreviewed; 911 AA.
AC K5BG91;
DT 09-JAN-2013, integrated into UniProtKB/TrEMBL.
DT 09-JAN-2013, sequence version 1.
DT 27-MAR-2024, entry version 53.
DE RecName: Full=Aconitate hydratase A {ECO:0000256|ARBA:ARBA00019378};
DE EC=4.2.1.3 {ECO:0000256|ARBA:ARBA00012926};
DE EC=4.2.1.99 {ECO:0000256|ARBA:ARBA00013250};
DE AltName: Full=(2R,3S)-2-methylisocitrate dehydratase {ECO:0000256|ARBA:ARBA00031613};
DE AltName: Full=(2S,3R)-3-hydroxybutane-1,2,3-tricarboxylate dehydratase {ECO:0000256|ARBA:ARBA00030846};
DE AltName: Full=Iron-responsive protein-like {ECO:0000256|ARBA:ARBA00031977};
DE AltName: Full=Probable 2-methyl-cis-aconitate hydratase {ECO:0000256|ARBA:ARBA00033025};
DE AltName: Full=RNA-binding protein {ECO:0000256|ARBA:ARBA00031081};
GN Name=acnA {ECO:0000313|EMBL:EKF23791.1};
GN ORFNames=C731_2159 {ECO:0000313|EMBL:EKF23791.1};
OS Mycolicibacterium hassiacum (strain DSM 44199 / CIP 105218 / JCM 12690 /
OS 3849) (Mycobacterium hassiacum).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=1122247 {ECO:0000313|EMBL:EKF23791.1, ECO:0000313|Proteomes:UP000006265};
RN [1] {ECO:0000313|EMBL:EKF23791.1, ECO:0000313|Proteomes:UP000006265}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 44199 / CIP 105218 / JCM 12690 / 3849
RC {ECO:0000313|Proteomes:UP000006265};
RX PubMed=23209251; DOI=10.1128/JB.01880-12;
RA Tiago I., Maranha A., Mendes V., Alarico S., Moynihan P.J., Clarke A.J.,
RA Macedo-Ribeiro S., Pereira P.J., Empadinhas N.;
RT "Genome sequence of Mycobacterium hassiacum DSM 44199, a rare source of
RT heat-stable mycobacterial proteins.";
RL J. Bacteriol. 194:7010-7011(2012).
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 -!- 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}.
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:EKF23791.1}.
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DR EMBL; AMRA01000054; EKF23791.1; -; Genomic_DNA.
DR AlphaFoldDB; K5BG91; -.
DR STRING; 1122247.GCA_000379865_00171; -.
DR PATRIC; fig|1122247.3.peg.2078; -.
DR eggNOG; COG1048; Bacteria.
DR UniPathway; UPA00223; UER00718.
DR UniPathway; UPA00946; -.
DR Proteomes; UP000006265; Unassembled WGS sequence.
DR GO; GO:0047456; F:2-methylisocitrate dehydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0003994; F:aconitate hydratase activity; IEA:UniProtKB-EC.
DR GO; GO:0051536; F:iron-sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006099; P:tricarboxylic acid cycle; IEA:UniProtKB-UniPathway.
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 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 Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Lyase {ECO:0000313|EMBL:EKF23791.1};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000006265}.
FT DOMAIN 45..573
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 702..832
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
SQ SEQUENCE 911 AA; 98721 MW; 4144329CE5CA3A1B CRC64;
MPGTEKLPYS LKVLAENLLR TEDGANVTKE HIEAIANWDP TAEPSVEIQF TPARVVMQDF
TGVPCVVDLA TMREAVAALG GDPEKVNPLA PAELVIDHSV ILDFFGRPDA FERNVELEYQ
RNGERYQFLR WGQTAFKDFK VVPPGTGIVH QVNIEYLARV TMVRDGVAYP DTCVGTDSHT
TMVNGLGVLG WGVGGIEAEA AMLGQPVSML IPRVVGFKLT REIRPGVTAT DVVLTVTEML
RKHGVVGKFV EFYGEGVAQV PLANRATLGN MSPEFGSTAA IFPIDAETIN YLRLTGRSEE
QIALVEAYAK EQGLWHDPAH EPAYSEYIEL DLSTVVPSIA GPKRPQDRIA LADAKTAFRK
DIHNYVEKPV ENPVPHTQLD EAVEESFPAS DPAALSFADD GAVDVRPSAA NGAQGRPSNP
VLVKSAERGE FVLDHGAVVV AGITSCTNTS NPEVMLGAAL LAKKAVEKGL STKPWVKTNM
APGSQVVSDY YTKAGLWPYL EKLGYYLGGY GCTTCIGNTG PLPEEISKAI NDNDLSVVAV
LSGNRNFEGR ISPDVKMNYL ASPPLVIAYG IAGTMDFDFE NDPLGKDPQG NDVFLRDIWP
SQEEIAEVIN SSITREMFAE SYADVFKGDE RWQNLPTPSG STFSWDPKST YVRKAPYFDG
MPAEPEPVTD IKGARVLALL GDSVTTDHIS PAGSIKRGTP AAQYLEANGV EPKDFNSLGS
RRGNHEVMIR GTFANIRLRN LLLDNVSGGY TRDFTQEGGP QAFIYDAAEN YKKAGIPLVV
IGGKEYGSGS SRDWAAKGTR LLGVRAVIAE SFERIHRSNL IGMGVIPLQF PAGESAASLK
LDGTEVYDIT GIEELNKGVT PRTVHVTATK ADGSKVEFDA VVRIDTPGEA DYYRNGGILQ
YVLRNMLKAS K
//
