ID A0A1C3K2K7_9BURK Unreviewed; 518 AA.
AC A0A1C3K2K7;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 38.
DE SubName: Full=Alanine racemase {ECO:0000313|EMBL:SBT25607.1};
DE EC=5.1.1.1 {ECO:0000313|EMBL:SBT25607.1};
GN ORFNames=ODI_03535 {ECO:0000313|EMBL:SBT25607.1}, ODI_R0593
GN {ECO:0000313|EMBL:SOE47010.1};
OS Orrella dioscoreae.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Alcaligenaceae; Orrella.
OX NCBI_TaxID=1851544 {ECO:0000313|EMBL:SBT25607.1, ECO:0000313|Proteomes:UP000078558};
RN [1] {ECO:0000313|EMBL:SBT25607.1, ECO:0000313|Proteomes:UP000078558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Orrdi1 {ECO:0000313|EMBL:SBT25607.1};
RA Kjaerup R.B., Dalgaard T.S., Juul-Madsen H.R.;
RL Submitted (JUN-2016) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:SOE47010.1, ECO:0000313|Proteomes:UP000078558}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Orrdi1 {ECO:0000313|EMBL:SOE47010.1};
RA de Groot N.N.;
RL Submitted (AUG-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600821-50};
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DR EMBL; FLRC01000021; SBT25607.1; -; Genomic_DNA.
DR EMBL; LT907988; SOE47010.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1C3K2K7; -.
DR STRING; 1851544.ODI_03535; -.
DR KEGG; odi:ODI_R0593; -.
DR Proteomes; UP000078558; Chromosome i.
DR Proteomes; UP000078558; Unassembled WGS sequence.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR InterPro; IPR000821; Ala_racemase.
DR InterPro; IPR009006; Ala_racemase/Decarboxylase_C.
DR InterPro; IPR011079; Ala_racemase_C.
DR InterPro; IPR001608; Ala_racemase_N.
DR InterPro; IPR020622; Ala_racemase_pyridoxalP-BS.
DR InterPro; IPR029066; PLP-binding_barrel.
DR NCBIfam; TIGR00492; alr; 1.
DR PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR PANTHER; PTHR30511:SF0; ALANINE RACEMASE, CATABOLIC-RELATED; 1.
DR Pfam; PF00842; Ala_racemase_C; 1.
DR Pfam; PF01168; Ala_racemase_N; 1.
DR PRINTS; PR00992; ALARACEMASE.
DR SMART; SM01005; Ala_racemase_C; 1.
DR SUPFAM; SSF50621; Alanine racemase C-terminal domain-like; 1.
DR SUPFAM; SSF51419; PLP-binding barrel; 1.
DR PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE 4: Predicted;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:SBT25607.1};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR600821-50};
KW Reference proteome {ECO:0000313|Proteomes:UP000078558}.
FT DOMAIN 373..515
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT REGION 1..64
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 292..314
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 13..27
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 245
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 452
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 137
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 518 AA; 54732 MW; E93B5ADBB3B77787 CRC64;
MGSSSTPQPA IASSSAAPPP PPPVVASAPS SSQHLGLLKG RAAKGAQPNR PLGKPLPVAE
SAGTSKPPVF ARANLARAKF WAKDSPIYAK IMTALNEPRI EASFAATLEV NLGNIRKNYR
KGADKLGAHV EAAAVIKADA YGLGATTVAK ALMQEGCRTF FVARTTEAIK LRSELRDEDH
PLADTVKIHV LDGLLAHVEP RVLVEYDISP VLNSPAQAKR WSDHAANSPT GKLPCILQFD
TGMNRAGMTE AEAETMIAQL SGTAGPDAAG SLEQERYAGL EVTHIMTHLA KAGEAAPRPG
EGNDATRQAG ETSQAQLARF ETLCQHFPQA KHSIGASSTV FLEPAFHKDM VRMGGTFHGQ
APFEADTNPL LPTITLVTSL SKIHQLKAGE GTGYGLRFTA HQDMPVATIP LGYADGLPRR
AHGNAPADAG QPEAFVLVEG RYRAPFVGAT SMDMSTIDLS AVPKAFHHEG ARVTVIGPHE
ASGQGITPDH FGDSEGTNAS ELQTKITSRV RKTYTDQA
//