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Database: UniProt
Entry: A0A1E7NAL3_KITAU
LinkDB: A0A1E7NAL3_KITAU
Original site: A0A1E7NAL3_KITAU 
ID   A0A1E7NAL3_KITAU        Unreviewed;       399 AA.
AC   A0A1E7NAL3; A0A8H9LTU0;
DT   18-JAN-2017, integrated into UniProtKB/TrEMBL.
DT   18-JAN-2017, sequence version 1.
DT   27-MAR-2024, entry version 38.
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=alr {ECO:0000313|EMBL:GGU91275.1};
GN   ORFNames=GCM10010502_50780 {ECO:0000313|EMBL:GGU91275.1}, HS99_0025750
GN   {ECO:0000313|EMBL:OEV37708.1};
OS   Kitasatospora aureofaciens (Streptomyces aureofaciens).
OC   Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC   Streptomycetaceae; Kitasatospora.
OX   NCBI_TaxID=1894 {ECO:0000313|EMBL:OEV37708.1, ECO:0000313|Proteomes:UP000037395};
RN   [1] {ECO:0000313|EMBL:OEV37708.1, ECO:0000313|Proteomes:UP000037395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10762 {ECO:0000313|EMBL:OEV37708.1}, and ATCC 10762 / DSM
RC   40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC 12843 / NCIMB 8234 /
RC   A-377 {ECO:0000313|Proteomes:UP000037395};
RA   Zhang J.E., Yang H., Guo J., Deng Z., Luo H., Luo M., Zhao B.;
RL   Submitted (JUL-2014) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|Proteomes:UP000037395}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10762 / DSM 40127 / CCM 3239 / JCM 4008 / LMG 5968 / NBRC
RC   12843 / NCIMB 8234 / A-377 {ECO:0000313|Proteomes:UP000037395};
RA   Gradnigo J.S., Johnson N., Somerville G.A.;
RT   "Sequencing, assembly and comparative genomics of S. aureofaciens ATCC
RT   10762.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:OEV37708.1}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 10762 {ECO:0000313|EMBL:OEV37708.1};
RA   Gradnigo J.S., Johnson N., Somerville G.A.;
RT   "Sequencing, Assembly and Comparative Genomics of S. aureofaciens ATCC
RT   10762.";
RL   Submitted (AUG-2016) to the EMBL/GenBank/DDBJ databases.
RN   [4] {ECO:0000313|EMBL:GGU91275.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 4434 {ECO:0000313|EMBL:GGU91275.1};
RX   PubMed=30832757;
RA   Wu L., Ma J.;
RT   "The Global Catalogue of Microorganisms (GCM) 10K type strain sequencing
RT   project: providing services to taxonomists for standard genome sequencing
RT   and annotation.";
RL   Int. J. Syst. Evol. Microbiol. 69:895-898(2019).
RN   [5] {ECO:0000313|EMBL:GGU91275.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=JCM 4434 {ECO:0000313|EMBL:GGU91275.1};
RA   Sun Q., Ohkuma M.;
RL   Submitted (SEP-2020) 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:OEV37708.1}.
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DR   EMBL; BMUB01000013; GGU91275.1; -; Genomic_DNA.
DR   EMBL; JPRF03000019; OEV37708.1; -; Genomic_DNA.
DR   RefSeq; WP_030280827.1; NZ_LBHA01000139.1.
DR   AlphaFoldDB; A0A1E7NAL3; -.
DR   GeneID; 33986016; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000037395; Unassembled WGS sequence.
DR   Proteomes; UP000610124; 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:UP000037395}.
FT   DOMAIN          262..389
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        48
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        283
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         149
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         331
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         48
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   399 AA;  41934 MW;  24CA0035EBF57605 CRC64;
     MTTANTTGTA TLTDGVRAEA TIDLAALRGN LAALQERVGS TAVMLAVKAD AYGHGAVECA
     REAVANGVGW LGCATPDEAL ALRAAGIRPE QARILCWLWT PGGPWREALR ADLDISVSGR
     WALEELLTAV RETGIPARVH LKADTGLGRN GCQPHDWPQL VAEVRRAEAA GLLKAVGIWS
     HFAAADEPGH PSIQAQLDSY RAALAHAELA GLRPEVRHLA NSPATLLLPE THFDLVRTGL
     AAYGLSPVPE VGSPADFGLR PVMALTARLA LVKHVPGGHG VSYGHHYVTP GPTTLGLVPV
     GYGDGVPRHA SGTGPVQIDG KWRTVAGRVA MDQFVVDLGG DTPEAGDEVL LFGNGERGEP
     TAEDWARASG SISYEIITRI GARVPRRYLG GSHDGSRRA
//
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