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Database: UniProt
Entry: U5MTY5_CLOSA
LinkDB: U5MTY5_CLOSA
Original site: U5MTY5_CLOSA 
ID   U5MTY5_CLOSA            Unreviewed;       380 AA.
AC   U5MTY5;
DT   22-JAN-2014, integrated into UniProtKB/TrEMBL.
DT   22-JAN-2014, sequence version 1.
DT   24-JAN-2024, entry version 56.
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=alr1 {ECO:0000313|EMBL:AGX44055.1};
GN   ORFNames=CLSA_c30890 {ECO:0000313|EMBL:AGX44055.1};
OS   Clostridium saccharobutylicum DSM 13864.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=1345695 {ECO:0000313|EMBL:AGX44055.1, ECO:0000313|Proteomes:UP000017118};
RN   [1] {ECO:0000313|EMBL:AGX44055.1, ECO:0000313|Proteomes:UP000017118}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 13864 {ECO:0000313|EMBL:AGX44055.1};
RX   PubMed=24285650;
RA   Poehlein A., Hartwich K., Krabben P., Ehrenreich A., Liebl W., Durre P.,
RA   Gottschalk G., Daniel R.;
RT   "Complete Genome Sequence of the Solvent Producer Clostridium
RT   saccharobutylicum NCP262 (DSM 13864).";
RL   Genome Announc. 1:e00997-13(2013).
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; CP006721; AGX44055.1; -; Genomic_DNA.
DR   RefSeq; WP_022747198.1; NZ_AYXL01000084.1.
DR   AlphaFoldDB; U5MTY5; -.
DR   GeneID; 55475445; -.
DR   KEGG; csb:CLSA_c30890; -.
DR   PATRIC; fig|1345695.10.peg.4547; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_9; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000017118; 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:UP000017118}.
FT   DOMAIN          245..373
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        38
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        266
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         314
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         38
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   380 AA;  42404 MW;  BE15017654260BA3 CRC64;
     MEKYFRSYAR IDLDAISHNI NEVKKRIGHG VKVMAVIKAD GYGHGATVLG DFLKNEVDYY
     GVATIEEAME LREYGIKVPI LILGYTSPSQ YLTLVENDIT QTVYNIEMAK EMSNAGEKCK
     KQAKIHIALD TGMTRIGFQP NEDGALAVKE IATFPSLNIE GLFTHFACAD EKDKSYSELQ
     IDRYDKFVEL LEEKDINIPI KHMCNSAGIM EFDHHRFDMV RSGIITYGLY PSEDVNKDAI
     KLKPALQWKT HVVNVKNVDS GHGVSYGATY ITKNKTKIAT ISIGYADGYP RALSSKAKVL
     IHGSYAPIIG RVCMDQMMID VTNIDNVEIE DEVTLVGQDG RNAISVEELA DIAGSFNYEF
     VCGIGKRVPR VYEGVEQECI
//
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