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Database: UniProt/TrEMBL
Entry: H2JB08_9CLOT
LinkDB: H2JB08_9CLOT
Original site: H2JB08_9CLOT 
ID   H2JB08_9CLOT            Unreviewed;       389 AA.
AC   H2JB08;
DT   21-MAR-2012, integrated into UniProtKB/TrEMBL.
DT   21-MAR-2012, sequence version 1.
DT   24-JAN-2024, entry version 67.
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=Clo1100_3695 {ECO:0000313|EMBL:AEY67814.1};
OS   Clostridium sp. BNL1100.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Clostridiaceae;
OC   Clostridium.
OX   NCBI_TaxID=755731 {ECO:0000313|EMBL:AEY67814.1, ECO:0000313|Proteomes:UP000007324};
RN   [1] {ECO:0000313|EMBL:AEY67814.1, ECO:0000313|Proteomes:UP000007324}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BNL1100 {ECO:0000313|EMBL:AEY67814.1,
RC   ECO:0000313|Proteomes:UP000007324};
RX   PubMed=23209234; DOI=10.1128/JB.01908-12;
RA   Li L.L., Taghavi S., Izquierdo J.A., van der Lelie D.;
RT   "Complete Genome Sequence of Clostridium sp. Strain BNL1100, a Cellulolytic
RT   Mesophile Isolated from Corn Stover.";
RL   J. Bacteriol. 194:6982-6983(2012).
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; CP003259; AEY67814.1; -; Genomic_DNA.
DR   RefSeq; WP_014315171.1; NC_016791.1.
DR   AlphaFoldDB; H2JB08; -.
DR   STRING; 755731.Clo1100_3695; -.
DR   KEGG; clb:Clo1100_3695; -.
DR   PATRIC; fig|755731.4.peg.3701; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_2_2_9; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000007324; 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}.
FT   DOMAIN          247..376
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        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         316
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   389 AA;  43217 MW;  0B93D2C5137FBB8D CRC64;
     MEYKLNRAWA EISLDNIAHN IREIRKITGK NAEIMGVVKA DAYGHGVMEV AKTLLENGAS
     RFAVSMLDEA IQLRRAGIEV PILILGFTDP IRASEIIEND VTQSVFSHDL AQALSDEAVR
     QGKKVKIHIK IDTGMSRIGF LPGYSAVKNV VEISRLPNII IEGLFTHFAT ADEKNREYTY
     TQFERFMSIC CELQRIGIHI PVKHCANSAA IIEYPEMHLD MVRPGIILYG MYPSDEVDKS
     KIDLKPAMTL KANVIMVKEV EKNTSISYGR IFTTGRTSKI ATIPIGYADG FNRMLSNKGK
     VLIHGEFAPV VGRICMDQCM VDITDIGCNV EVGDEIVLIG SQGQNNITAE DVAHTIGMIN
     YELVCIVGKR IPRAFVKDGK ISKILNYLI
//
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