ID A0A149QH68_9PROT Unreviewed; 376 AA.
AC A0A149QH68;
DT 08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT 08-JUN-2016, sequence version 1.
DT 24-JAN-2024, entry version 36.
DE RecName: Full=Alanine racemase {ECO:0000256|ARBA:ARBA00013089, ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089, ECO:0000256|HAMAP-Rule:MF_01201};
GN ORFNames=AD928_04490 {ECO:0000313|EMBL:KXU96649.1};
OS Acetobacter cerevisiae.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=178900 {ECO:0000313|EMBL:KXU96649.1, ECO:0000313|Proteomes:UP000075473};
RN [1] {ECO:0000313|EMBL:KXU96649.1, ECO:0000313|Proteomes:UP000075473}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 1625 {ECO:0000313|EMBL:KXU96649.1,
RC ECO:0000313|Proteomes:UP000075473};
RA Li L., Cleenwerck I., De Vuyst L., Vandamme P.;
RT "Improved classification and identification of acetic acid bacteria using
RT matrix-assisted laser desorption/ionization time-of-flight mass
RT spectrometry; Gluconobacter nephelii and Gluconobacter uchimurae are later
RT heterotypic synonyms of Gluconobacter japonicus and Gluconobacter oxydans,
RT respectively.";
RL Submitted (JUN-2015) 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|ARBA:ARBA00000316, ECO:0000256|HAMAP-
CC 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.
CC {ECO:0000256|ARBA:ARBA00007880, ECO:0000256|HAMAP-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:KXU96649.1}.
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DR EMBL; LHZA01000126; KXU96649.1; -; Genomic_DNA.
DR RefSeq; WP_062248603.1; NZ_LHZA01000126.1.
DR AlphaFoldDB; A0A149QH68; -.
DR PATRIC; fig|178900.5.peg.1349; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000075473; 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:UP000075473}.
FT DOMAIN 239..371
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 39
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 260
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 311
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 39
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 376 AA; 39808 MW; F0AC72E7728AC338 CRC64;
MDRDGWEGGR LLINLAAIAE NYAQLSARVS PAECGAAVKA NAYGLGLKEV GQTLYEAGCR
TFFVAHLAEG AALRPLVGED SRIFVLHGPP PGTANACLTH NLLPVLNSLQ QVQEWQALAH
AQGHPLAAAL QVDSGMSRFG LTEAEVDYLA TQPQALAGIE VTLVMSHLAC ADTPDHPLNR
QQLNAFVKLK LRLPAAPASL AASSGIFLGP EWHFDLVRPG AALYGIAPTA GQPNPMHATL
RLQARVIQTR QVPAGASVGY GAAFTARQPT PVALLGIGYG DGFPRRLGQK GFVIYPDWPD
IKLPIIGRIS MDSLAVDLSP LVAAGVALPP AGAVFDLIGP HAPLDDVAHL ADTIAYELLT
DLGARYHRLH YDPRKG
//
