ID A0A1H0B339_9BACI Unreviewed; 679 AA.
AC A0A1H0B339;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE SubName: Full=Aconitate hydratase {ECO:0000313|EMBL:SDN39753.1};
GN ORFNames=SAMN05216498_2188 {ECO:0000313|EMBL:SDN39753.1};
OS Tenuibacillus multivorans.
OC Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Tenuibacillus.
OX NCBI_TaxID=237069 {ECO:0000313|EMBL:SDN39753.1, ECO:0000313|Proteomes:UP000199334};
RN [1] {ECO:0000313|EMBL:SDN39753.1, ECO:0000313|Proteomes:UP000199334}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.3442 {ECO:0000313|EMBL:SDN39753.1,
RC ECO:0000313|Proteomes:UP000199334};
RA de Groot N.N.;
RL Submitted (OCT-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- SUBUNIT: Monomer. {ECO:0000256|ARBA:ARBA00011245}.
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DR EMBL; FNIG01000004; SDN39753.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H0B339; -.
DR STRING; 237069.SAMN05216498_2188; -.
DR UniPathway; UPA00223; -.
DR Proteomes; UP000199334; Unassembled WGS sequence.
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 Gene3D; 3.30.499.10; Aconitase, domain 3; 2.
DR Gene3D; 3.20.19.10; Aconitase, domain 4; 1.
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; IPR036008; Aconitase_4Fe-4S_dom.
DR InterPro; IPR006250; Aconitase_put.
DR InterPro; IPR000573; AconitaseA/IPMdHydase_ssu_swvl.
DR NCBIfam; TIGR01342; acon_putative; 1.
DR PANTHER; PTHR43160; ACONITATE HYDRATASE B; 1.
DR PANTHER; PTHR43160:SF3; ACONITATE HYDRATASE, MITOCHONDRIAL; 1.
DR Pfam; PF00330; Aconitase; 2.
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 4: Predicted;
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW Reference proteome {ECO:0000313|Proteomes:UP000199334};
KW Tricarboxylic acid cycle {ECO:0000256|ARBA:ARBA00022532}.
FT DOMAIN 35..312
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 312..434
FT /note="Aconitase/3-isopropylmalate dehydratase large
FT subunit alpha/beta/alpha"
FT /evidence="ECO:0000259|Pfam:PF00330"
FT DOMAIN 541..609
FT /note="Aconitase A/isopropylmalate dehydratase small
FT subunit swivel"
FT /evidence="ECO:0000259|Pfam:PF00694"
FT REGION 394..417
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 396..411
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 679 AA; 74258 MW; 2C9123853CEC94E7 CRC64;
MGFWGSFYIE TFLNVDMYGN FRKGFLLVKL NLAQKLIKEH LVSGEMDPGT EIGLKIDQTL
CQDATGTMVM LELEAMGVDQ AKTEASAQYV DHNLIQDDHR NPDDHLFLRS AAKRFGLYFS
RPGNGVSHPV QMQKLAKPGK TLLGSDSHTC ANGCMGMLAM GAGGIDVAMA IAGEPFYVKM
PQIWGVKVTG ELPDWVSAKD VILEMLRRHD VKGGVGKILE FYGPGLKNLT AMDRHVIANM
GAELGATATV FPSDNEIKRF LKTQDREEDW VELTADNGAE YDLHDEIDLS SLEPLIAKPS
SPGNVVPVSE LAGESIYQSY IGSSANPGYR DFAIAAEIVK GKSIAQGLSF DINPSSRQIL
TQLVDNGHIA SLLSSGARLH QAGCNGCIGM GQAPASGRNS LRTTPRNFPG RSGTKEDSVF
LCSPETAAAS ALTGVITDPR TLEMDYPDIK EPKVDFEKEE GMLEEPIPES EGINAELDKG
PNIKSIPKLA PIENNFEVPI LLKMGDNIST DEILAGGSRV LPYRSNLQRI STFTFEIVDD
TYYERAMKQK DDGGHAVVAG FNYGQGSSRE HAALAPRHLG LKVVLVKDFA RIHLQNLINF
GVLPLTFVNE DDLDKLESGD ILQFENVRDN LPNSNEFEVG IKDKDEKIKV KHSLTDRHLD
IILAGGIINW IKNKQESGV
//
