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Database: UniProt/TrEMBL
Entry: A0A075LGU1_9BACI
LinkDB: A0A075LGU1_9BACI
Original site: A0A075LGU1_9BACI 
ID   A0A075LGU1_9BACI        Unreviewed;       390 AA.
AC   A0A075LGU1;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 44.
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=GZ22_01835 {ECO:0000313|EMBL:AIF65521.1};
OS   Terribacillus goriensis.
OC   Bacteria; Bacillota; Bacilli; Bacillales; Bacillaceae; Terribacillus.
OX   NCBI_TaxID=386490 {ECO:0000313|EMBL:AIF65521.1, ECO:0000313|Proteomes:UP000027980};
RN   [1] {ECO:0000313|EMBL:AIF65521.1, ECO:0000313|Proteomes:UP000027980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MP602 {ECO:0000313|EMBL:AIF65521.1,
RC   ECO:0000313|Proteomes:UP000027980};
RA   Wang Y., Lu P., Zhang L.;
RT   "Complete genome sequence of a moderately halophilic bacterium
RT   Terribacillus aidingensis MP602, isolated from Cryptomeria fortunei in
RT   Tianmu mountain in China.";
RL   Submitted (JUL-2014) 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}.
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DR   EMBL; CP008876; AIF65521.1; -; Genomic_DNA.
DR   RefSeq; WP_038558134.1; NZ_CP008876.1.
DR   AlphaFoldDB; A0A075LGU1; -.
DR   KEGG; tap:GZ22_01835; -.
DR   HOGENOM; CLU_028393_2_1_9; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000027980; 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; 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:UP000027980}.
FT   DOMAIN          247..372
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        41
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        268
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         137
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         315
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         41
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   390 AA;  43469 MW;  FF5DBBC2245A3923 CRC64;
     MRVDNFYRDS WVEINLDHVE YNIKQLAAHI GEDKGIYAVV KANAYGHGYT QVAQAALDAG
     ASALAVAFLD EALHLRKAGI QAAILVLGAT RAEDAAIAAD HDISLTFYRK DWLEAVRAEQ
     FRKPLQLHMK LDTGMGRLGF RTEDDIRSAM PLLDTPSLIL EGVYTHFATA DEADLSYFEG
     QRSKFDELFK VLREEWPDSV IVHTDNSAAS MRFAADESDF VRFGIGMYGL YPSSTVKEEH
     PIALRQAFSL HSKLVHVKQL EAHEAVSYGA TYETDKPEWI GTLPIGYADG WIRKMQGFEV
     LVDGKRMPIV GRVCMDQCMV KLDKDYPVGT EVVLIGSQLD AFISVDEAAD WVDTINYEIP
     CLIGARMPRV YKRSGQIVET ANALNPGESL
//
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