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Database: UniProt
Entry: A0A413I4G5_9FIRM
LinkDB: A0A413I4G5_9FIRM
Original site: A0A413I4G5_9FIRM 
ID   A0A413I4G5_9FIRM        Unreviewed;       391 AA.
AC   A0A413I4G5;
DT   08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT   08-MAY-2019, sequence version 1.
DT   24-JAN-2024, entry version 14.
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=alr {ECO:0000313|EMBL:RGY02355.1};
GN   ORFNames=DXA57_03550 {ECO:0000313|EMBL:RGY02355.1};
OS   Blautia sp. OF03-15BH.
OC   Bacteria; Bacillota; Clostridia; Eubacteriales; Lachnospiraceae; Blautia.
OX   NCBI_TaxID=2292287 {ECO:0000313|EMBL:RGY02355.1, ECO:0000313|Proteomes:UP000285119};
RN   [1] {ECO:0000313|EMBL:RGY02355.1, ECO:0000313|Proteomes:UP000285119}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=OF03-15BH {ECO:0000313|EMBL:RGY02355.1,
RC   ECO:0000313|Proteomes:UP000285119};
RA   Zou Y., Xue W., Luo G.;
RT   "A genome reference for cultivated species of the human gut microbiota.";
RL   Submitted (AUG-2018) 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}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:RGY02355.1}.
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DR   EMBL; QSCM01000002; RGY02355.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A413I4G5; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000285119; 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   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; 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.
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:UP000285119}.
FT   DOMAIN          249..377
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        40
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        270
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         139
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         318
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         40
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   391 AA;  43959 MW;  A9E9183528181798 CRC64;
     MKETEAMRIY AAIDLDACRK NIDAMFAKLR PETKMTLVIK TDGYGHGALP VARLGETMER
     VWGYAVATAQ EAFYLRRNGI RKPILILGYT FEGDYLKMVE EEIRPVVFRY ETAAAFSRAA
     KEAGKTVHIH IGLDTGMHRI GFSDTMESIG EIQKIRQLEQ VELEGIFTHF ARADEEDKTF
     ARAQLLRFVS FVTKLEKKGI TFQLRHAANS ASIMEFPEAQ IDMVRAGITI YGIYPSEEMK
     PENLPLEPMM ELKSRIVLIK EIAPRDAVSY GGTFVAEKNM RIATISAGYG DGYPRSLSNK
     GFVLIHGKKA PILGRICMDQ FMVDVTDIPE AAELEEVTLM GKDGEAFLPV TALSELAGRF
     PYEFVCDIGK RVPRVYYQDG KIVEIVDELV K
//
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