ID A0A1B3ZAY0_9SPHN Unreviewed; 343 AA.
AC A0A1B3ZAY0;
DT 02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT 02-NOV-2016, sequence version 1.
DT 24-JAN-2024, entry version 29.
DE RecName: Full=alanine racemase {ECO:0000256|ARBA:ARBA00013089};
DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089};
GN ORFNames=AWL63_12030 {ECO:0000313|EMBL:AOH84586.1};
OS Sphingomonas panacis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Sphingomonas.
OX NCBI_TaxID=1560345 {ECO:0000313|EMBL:AOH84586.1, ECO:0000313|Proteomes:UP000094256};
RN [1] {ECO:0000313|EMBL:AOH84586.1, ECO:0000313|Proteomes:UP000094256}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DCY99 {ECO:0000313|EMBL:AOH84586.1,
RC ECO:0000313|Proteomes:UP000094256};
RA Kim Y.J., Yang D.C., Sing P.;
RT "Complete genome and mega plasmid sequence of Sphingomonas panacis DCY99
RT elicits systemic resistance in rice to Xanthomonas oryzae.";
RL Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000316};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|PIRSR:PIRSR600821-50};
CC -!- SIMILARITY: Belongs to the alanine racemase family.
CC {ECO:0000256|ARBA:ARBA00007880}.
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DR EMBL; CP014168; AOH84586.1; -; Genomic_DNA.
DR RefSeq; WP_069205136.1; NZ_CP014168.1.
DR AlphaFoldDB; A0A1B3ZAY0; -.
DR STRING; 1560345.AWL63_12030; -.
DR KEGG; span:AWL63_12030; -.
DR OrthoDB; 9813814at2; -.
DR Proteomes; UP000094256; Chromosome.
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 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR600821-50}.
FT DOMAIN 221..342
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT BINDING 126
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 290
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 35
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 343 AA; 36330 MW; 325C9E626B74341A CRC64;
MNAPHRLRLD SAALVANWRA LAALSGPAAC GAAIKADGYG LGAVEVARRL AQAGCRDFFV
ATWAEAEALA PLGLPVAVLH GVREEDMATA PQGFAWPVLN TERQVARWRA AGGGRCDVMV
DTGMSRLGIA AAAVCDGTLD GLEIGTLMSH LASADEDSPL NGRQLAAFTS LKGHHPAKRM
SLANSAAIAF GRDYAFDLTR PGLALYGGVP REELAGTLRQ VVTPEAQILQ RRRLQPGDVI
GYNALFTAER STEVAILNLG YADGYWRGFS QRGAAHHGEA RLPVLGRVSM DLTAIAVDAV
PDLAEGDWVA IDYALPEAAA LSGMSQYELL TGLGKRFDRM WVG
//