ID A0A2M9CZ98_9CELL Unreviewed; 443 AA.
AC A0A2M9CZ98;
DT 25-APR-2018, integrated into UniProtKB/TrEMBL.
DT 25-APR-2018, sequence version 1.
DT 24-JAN-2024, entry version 22.
DE RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN ORFNames=CLV28_0431 {ECO:0000313|EMBL:PJJ77217.1};
OS Sediminihabitans luteus.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Cellulomonadaceae;
OC Sediminihabitans.
OX NCBI_TaxID=1138585 {ECO:0000313|EMBL:PJJ77217.1, ECO:0000313|Proteomes:UP000231693};
RN [1] {ECO:0000313|EMBL:PJJ77217.1, ECO:0000313|Proteomes:UP000231693}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 25478 {ECO:0000313|EMBL:PJJ77217.1,
RC ECO:0000313|Proteomes:UP000231693};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): From Individual Species to Whole Genera.";
RL Submitted (NOV-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
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|HAMAP-Rule:MF_01201};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family. {ECO:0000256|HAMAP-
CC Rule:MF_01201}.
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:PJJ77217.1}.
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DR EMBL; PGFE01000001; PJJ77217.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2M9CZ98; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000231693; Unassembled WGS sequence.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR HAMAP; MF_01201; Ala_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, ECO:0000256|HAMAP-Rule:MF_01201};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}; Reference proteome {ECO:0000313|Proteomes:UP000231693}.
FT DOMAIN 258..410
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT REGION 413..443
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 428..443
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 44
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 279
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 145
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 347
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 44
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 443 AA; 44974 MW; B69EB5C8AB9CFF6C CRC64;
MSDDRVSTST TFPARAVVDL DAIAGNVAAL AAHAPSAAVM AVVKADAYGH GLVPAARAAL
AGGATWLGTA QVAEALALRA AGITAADARV LTWLYAPGAP LAALLEADVD VSVHADWALA
EVVAAARATG RVARVHLKVD TGLGRNGLVP PDLARVLPDA MTARAEGLID VVGVWSHLAF
ADEPGNPTVL HQAEVFDDAV RLVEQAGAAL EVRHLANSAA TLTAPRMHYD LVRPGIAVYG
LTPVPQIASS ADHGLTPAMT LEARLANVKR VPAGQGVSYA HRYVTTQETT LGVVPLGYAD
GIPRHASGEP GHPGGPVLVG GADAADAASG ALPDGARVLH VAGRVCMDQL VLDLGPYATE
RAGDVVTLFG AGAGLAHGGA PTAQDWADAA GTISYEIVTR LGARVPRTYV GGLAGDLREQ
GPDGESSRGS GPHDEVPYDR GTA
//
