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Database: UniProt/TrEMBL
Entry: A0A0F2KMP5_9PROT
LinkDB: A0A0F2KMP5_9PROT
Original site: A0A0F2KMP5_9PROT 
ID   A0A0F2KMP5_9PROT        Unreviewed;       382 AA.
AC   A0A0F2KMP5;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-SEP-2017, entry version 20.
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=VY88_26875 {ECO:0000313|EMBL:KJR62532.1};
OS   Azospirillum thiophilum.
OC   Bacteria; Proteobacteria; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Azospirillum.
OX   NCBI_TaxID=528244 {ECO:0000313|EMBL:KJR62532.1, ECO:0000313|Proteomes:UP000033623};
RN   [1] {ECO:0000313|EMBL:KJR62532.1, ECO:0000313|Proteomes:UP000033623}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 21654 {ECO:0000313|EMBL:KJR62532.1,
RC   ECO:0000313|Proteomes:UP000033623};
RA   Kwak Y., Shin J.-H.;
RT   "Genome sequence of Azospirillum thiophilum strain DSM 21654T.";
RL   Submitted (MAR-2015) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an
CC       EMBL/GenBank/DDBJ whole genome shotgun (WGS) entry which is
CC       preliminary data. {ECO:0000313|EMBL:KJR62532.1}.
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DR   EMBL; LAEL01000005; KJR62532.1; -; Genomic_DNA.
DR   RefSeq; WP_045585089.1; NZ_LAEL01000005.1.
DR   EnsemblBacteria; KJR62532; KJR62532; VY88_26875.
DR   KEGG; ati:AL072_29780; -.
DR   PATRIC; fig|528244.3.peg.5597; -.
DR   KO; K01775; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000033623; 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   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:UP000033623};
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}.
FT   DOMAIN      254    380       Ala_racemase_C. {ECO:0000259|SMART:
FT                                SM01005}.
FT   ACT_SITE     51     51       Proton acceptor; specific for D-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   ACT_SITE    275    275       Proton acceptor; specific for L-alanine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201}.
FT   BINDING     153    153       Substrate. {ECO:0000256|HAMAP-Rule:
FT                                MF_01201, ECO:0000256|PIRSR:PIRSR600821-
FT                                52}.
FT   BINDING     323    323       Substrate; via amide nitrogen.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-52}.
FT   MOD_RES      51     51       N6-(pyridoxal phosphate)lysine.
FT                                {ECO:0000256|HAMAP-Rule:MF_01201,
FT                                ECO:0000256|PIRSR:PIRSR600821-50}.
SQ   SEQUENCE   382 AA;  39899 MW;  2EA0A44D177C821F CRC64;
     MPAPEPVPQP VPSDPAARAG AFLTVDLAAV VANWTQLRDR VAPAECSAVV KADAYGLGVA
     RVVPALAAAG CRTFVVAQFE EALAVRRALE PVAPDAQVFS LGGLPAGCEG DFIANRILPV
     LNHLGEIAAW GAFAALRGGA LPAVIHIDTG MNRLGLGPDE LDALAAEPAR LAGIDVRYWM
     THLACADEFD NPMTGAQLDR FRSALARLPK AKASFANSSG IFHGPDHHFD LARPGCALYG
     VNPTPHLPNP MRGTVRLDAR LLQVRNCTPA MTVGYGAAHA VTGPARIATI GVGYADGYLR
     ALGGKGQVFV DGVAAPIVGR ISMDLITIDV SGLPEQVAHA GRMVELIGPS RPVDRVAAEG
     GTIGYEILTS LGRRYHRVYL GG
//
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