ID A0A140L0I7_9CLOT Unreviewed; 736 AA.
AC A0A140L0I7;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 27-MAR-2024, entry version 22.
DE SubName: Full=D-ornithine 4,5-aminomutase subunit beta {ECO:0000313|EMBL:KXG74062.1};
DE EC=5.4.3.5 {ECO:0000313|EMBL:KXG74062.1};
GN Name=oraE {ECO:0000313|EMBL:KXG74062.1};
GN ORFNames=AN619_26720 {ECO:0000313|EMBL:KXG74062.1};
OS Thermotalea metallivorans.
OC Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC Thermotalea.
OX NCBI_TaxID=520762 {ECO:0000313|EMBL:KXG74062.1, ECO:0000313|Proteomes:UP000070456};
RN [1] {ECO:0000313|EMBL:KXG74062.1, ECO:0000313|Proteomes:UP000070456}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=B2-1 {ECO:0000313|EMBL:KXG74062.1,
RC ECO:0000313|Proteomes:UP000070456};
RA Patel B.K.;
RT "Draft genome sequence of the thermoanaerobe Thermotalea metallivorans, an
RT isolate from the runoff channel of the Great Artesian Basin, Australia.";
RL Submitted (DEC-2015) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=adenosylcob(III)alamin; Xref=ChEBI:CHEBI:18408;
CC Evidence={ECO:0000256|ARBA:ARBA00001922};
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:KXG74062.1}.
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DR EMBL; LOEE01000065; KXG74062.1; -; Genomic_DNA.
DR RefSeq; WP_068557732.1; NZ_LOEE01000065.1.
DR AlphaFoldDB; A0A140L0I7; -.
DR STRING; 520762.AN619_26720; -.
DR PATRIC; fig|520762.4.peg.2948; -.
DR OrthoDB; 9759220at2; -.
DR Proteomes; UP000070456; Unassembled WGS sequence.
DR GO; GO:0031419; F:cobalamin binding; IEA:UniProtKB-KW.
DR GO; GO:0047831; F:D-ornithine 4,5-aminomutase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0046983; F:protein dimerization activity; IEA:InterPro.
DR Gene3D; 3.40.50.280; Cobalamin-binding domain; 1.
DR Gene3D; 3.20.20.440; D-Lysine 5,6-aminomutase alpha subunit; 1.
DR Gene3D; 3.30.30.60; D-lysine 5,6-aminomutase beta subunit KamE, N-terminal domain; 1.
DR InterPro; IPR016176; Cbl-dep_enz_cat.
DR InterPro; IPR006158; Cobalamin-bd.
DR InterPro; IPR036724; Cobalamin-bd_sf.
DR InterPro; IPR028991; KamE_N.
DR InterPro; IPR036843; KamE_N_sf.
DR InterPro; IPR015130; Lys-AminoMut_A.
DR InterPro; IPR037086; Lys-AminoMut_asu_sf.
DR NCBIfam; NF040743; ornith_mutase_E; 1.
DR Pfam; PF02310; B12-binding; 1.
DR Pfam; PF09043; Lys-AminoMut_A; 1.
DR Pfam; PF16554; OAM_dimer; 1.
DR SUPFAM; SSF52242; Cobalamin (vitamin B12)-binding domain; 1.
DR SUPFAM; SSF51703; Cobalamin (vitamin B12)-dependent enzymes; 1.
DR PROSITE; PS51332; B12_BINDING; 1.
PE 4: Predicted;
KW Cobalamin {ECO:0000256|ARBA:ARBA00022628};
KW Cobalt {ECO:0000256|ARBA:ARBA00023285};
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:KXG74062.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000070456}.
FT DOMAIN 598..735
FT /note="B12-binding"
FT /evidence="ECO:0000259|PROSITE:PS51332"
SQ SEQUENCE 736 AA; 82511 MW; 012EAEAB5521C455 CRC64;
MELKINEKIH IKEILKNLEN YRPKRRGWVW RDKVESLQMG PFTYKNCSKP LKNSVPLPSA
KYFGDIDPQP DYTITTEIAS GRFEDDIRRM RMAAWHGADH IMVIRTAGQS HFDGLIEGTP
QGIGGIPITR KQVRAQRKAL DMIEEEVGRP INYHSYVSGV AGPDIAVMFA EEGVNGAHQD
PQYNVLYRNI NMIRSFVDAA ESKKMMTWAD MAQIDGAHNA NATAREAWKV MPELMVQHAI
NAMYSVKVGM KKSNICLSTV PPTAPPAPCM KLDLPYAVAL RDLFSEYRMR AQMNTKYMES
STREATVTHV LNLMISRLTS ADIQSTITPD EGRNVPWHIY NMEACDTAKQ ALVGMDALLD
MVELKKEGYL PEKVRELKER AVLFLEEILE VGGYFKAVEE GFFVDSGYYP ERNGDGIVRK
IDGGIGAGTV FERDEDYFAP VTAHFGYNNV AQYDPNAVEN PSALIGGCTF EVPEKIVYID
ELDETDNVNV RLEETKELRE TSKIKPEVEW TGDGIVQLDL FLPTSRRVAE FAAIEIGKKM
GLADVEVIHK EVMHPSEGTR IQLKGRVEFA IDTNALVIPP EPEVMTEQEI REDIAARPMK
IVAATVGEDE HSVGLREIID IKHGGIEKYG IECHYLGTSV PVEKLVDAAI ELNADAILAS
TIISHDDIHY KNMRRIHELC VEKGIRDKIM IACGGTQVTP ELAVKQGVDA GFGRGSKGIH
VATFLVKRRR EMHHEN
//
