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Database: UniProt/TrEMBL
Entry: A0A1B1MWG6_9BACL
LinkDB: A0A1B1MWG6_9BACL
Original site: A0A1B1MWG6_9BACL 
ID   A0A1B1MWG6_9BACL        Unreviewed;       392 AA.
AC   A0A1B1MWG6;
DT   02-NOV-2016, integrated into UniProtKB/TrEMBL.
DT   02-NOV-2016, sequence version 1.
DT   27-SEP-2017, entry version 7.
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=AWM70_02120 {ECO:0000313|EMBL:ANS73523.1};
OS   Paenibacillus yonginensis.
OC   Bacteria; Firmicutes; Bacilli; Bacillales; Paenibacillaceae;
OC   Paenibacillus.
OX   NCBI_TaxID=1462996 {ECO:0000313|EMBL:ANS73523.1, ECO:0000313|Proteomes:UP000092573};
RN   [1] {ECO:0000313|EMBL:ANS73523.1, ECO:0000313|Proteomes:UP000092573}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DCY84 {ECO:0000313|EMBL:ANS73523.1,
RC   ECO:0000313|Proteomes:UP000092573};
RA   Kim Y.J., Yang D.C., Sukweenadhi J.;
RT   "Complete Genome Sequence of Paenibacillus yonginensis DCY84, a novel
RT   Plant Growth-Promoting Bacteria with Elicitation of Induced Systemic
RT   Resistance.";
RL   Submitted (JAN-2016) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-
CC       alanine. May also act on other amino acids. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- CATALYTIC ACTIVITY: L-alanine = D-alanine. {ECO:0000256|HAMAP-
CC       Rule:MF_01201, ECO:0000256|SAAS:SAAS00630646}.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_01201,
CC         ECO:0000256|PIRSR:PIRSR600821-50,
CC         ECO:0000256|SAAS:SAAS00758845};
CC   -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-
CC       alanine from L-alanine: step 1/1. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
CC   -!- SIMILARITY: Belongs to the alanine racemase family.
CC       {ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|SAAS:SAAS00630654}.
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DR   EMBL; CP014167; ANS73523.1; -; Genomic_DNA.
DR   RefSeq; WP_068693949.1; NZ_CP014167.1.
DR   EnsemblBacteria; ANS73523; ANS73523; AWM70_02120.
DR   KEGG; pyg:AWM70_02120; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000092573; 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   Gene3D; 2.40.37.10; -; 1.
DR   Gene3D; 3.20.20.10; -; 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   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; SSF50621; 1.
DR   SUPFAM; SSF51419; SSF51419; 1.
DR   TIGRFAMs; TIGR00492; alr; 1.
DR   PROSITE; PS00395; ALANINE_RACEMASE; 1.
PE   3: Inferred from homology;
KW   Complete proteome {ECO:0000313|Proteomes:UP000092573};
KW   Isomerase {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|SAAS:SAAS00630647};
KW   Pyridoxal phosphate {ECO:0000256|HAMAP-Rule:MF_01201,
KW   ECO:0000256|PIRSR:PIRSR600821-50, ECO:0000256|SAAS:SAAS00722456};
KW   Reference proteome {ECO:0000313|Proteomes:UP000092573}.
FT   DOMAIN      247    379       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     39     39       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    268    268       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     138    138       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     316    316       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      39     39       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   392 AA;  43543 MW;  8D59148F0FFE5188 CRC64;
     MQVNYRPTVA EIDLDAMESN YLALRQSLPE GMKLLICVKA NAYGHGAVHV AEEMQRLKAD
     YLSVAFLDEA LELRAAGITM PILVLGYTPP EGVRTAWDHG ITICIFDEEV LEAARRLGPE
     ASKSRLKVHI KVDTGMGRIG LLPDEAPAFV QQAVSVPGIE VEGLFTHFST ADEKDKSYTL
     EQYRRFQDVT DALKELQIKV PIIHTGNSAT AIDLPELSFD MVRVGIAIYG LYPSDEVRSQ
     NVKLIPVLSL KTRLSYVKEL PPGWGISYGK RYETQNWEKI GTLPVGYADG YSRMLGGKAH
     VLIRGRRVPV VGTICMDQCM VSLQDFKDNG EQIQVGEEAV LIGRQQGGEI SADELASWLG
     TIHYEVICMI AHRVPRVYKK AGRQDEIVNP LF
//
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