GenomeNet

Database: UniProt/TrEMBL
Entry: A0A077LH84_9PSED
LinkDB: A0A077LH84_9PSED
Original site: A0A077LH84_9PSED 
ID   A0A077LH84_9PSED        Unreviewed;       357 AA.
AC   A0A077LH84;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 43.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   Name=dadX {ECO:0000313|EMBL:BAP42313.1};
GN   ORFNames=PSCI_1611 {ECO:0000313|EMBL:BAP42313.1};
OS   Pseudomonas sp. StFLB209.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP42313.1, ECO:0000313|Proteomes:UP000031652};
RN   [1] {ECO:0000313|EMBL:BAP42313.1, ECO:0000313|Proteomes:UP000031652}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=StFLB209 {ECO:0000313|EMBL:BAP42313.1,
RC   ECO:0000313|Proteomes:UP000031652};
RX   PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA   Morohoshi T., Kato T., Someya N., Ikeda T.;
RT   "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT   sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL   Genome Announc. 2:e01037-e01014(2014).
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   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; AP014637; BAP42313.1; -; Genomic_DNA.
DR   RefSeq; WP_045485098.1; NZ_AP014637.1.
DR   AlphaFoldDB; A0A077LH84; -.
DR   STRING; 1028989.PSCI_1611; -.
DR   KEGG; pses:PSCI_1611; -.
DR   HOGENOM; CLU_028393_1_0_6; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000031652; Chromosome.
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; cd06827; PLPDE_III_AR_proteobact; 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:UP000031652}.
FT   DOMAIN          232..355
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        33
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        253
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         129
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         301
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         33
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   357 AA;  38748 MW;  CC46FDCCFF6AEF0D CRC64;
     MRPARALIDL NALRHNYRLA RQHSGARALA VIKADAYGHG AVRVAQALQS EADGFAVACI
     EEALELRAAG VSGPILLLEG FFEAQELDLI VEHDFWCVVH SQWQIEAIER TAVGKPLTLW
     LKLDSGMHRV GLFPADYQAA YQRLLASGKV ADIVLMSHFA RADELDCPRS AEQLAVFEAA
     RQGLKALTSL NNSPALLGWP QINSDWVRPG IMLYGATPFE QAHPLADQLQ AVMTLESKVI
     SVRELPAGEP VGYGASWITD RPSRIGVVAM GYADGYPRHA PTGTPVIIDG QAARLVGRVS
     MDMLCVELTD LPAAGLGSHI EFWGPNLSAS TVAAHAGTIP YQLFCNLKRV PRRYSEG
//
DBGET integrated database retrieval system