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Database: UniProt
Entry: A0A0Q8UQZ3_9MICO
LinkDB: A0A0Q8UQZ3_9MICO
Original site: A0A0Q8UQZ3_9MICO 
ID   A0A0Q8UQZ3_9MICO        Unreviewed;       350 AA.
AC   A0A0Q8UQZ3;
DT   20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT   20-JAN-2016, sequence version 1.
DT   24-JAN-2024, entry version 34.
DE   SubName: Full=Alanine racemase {ECO:0000313|EMBL:KRC47430.1};
GN   ORFNames=ASE16_17275 {ECO:0000313|EMBL:KRC47430.1};
OS   Leifsonia sp. Root227.
OC   Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Microbacteriaceae;
OC   Leifsonia.
OX   NCBI_TaxID=1736496 {ECO:0000313|EMBL:KRC47430.1, ECO:0000313|Proteomes:UP000051819};
RN   [1] {ECO:0000313|EMBL:KRC47430.1, ECO:0000313|Proteomes:UP000051819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root227 {ECO:0000313|EMBL:KRC47430.1,
RC   ECO:0000313|Proteomes:UP000051819};
RA   Gilbert D.G.;
RL   Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:KRC47430.1, ECO:0000313|Proteomes:UP000051819}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Root227 {ECO:0000313|EMBL:KRC47430.1,
RC   ECO:0000313|Proteomes:UP000051819};
RA   Schulze-Lefert P.;
RT   "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL   Submitted (NOV-2015) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600821-50};
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:KRC47430.1}.
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DR   EMBL; LMIO01000004; KRC47430.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A0Q8UQZ3; -.
DR   STRING; 1736496.ASE16_17275; -.
DR   Proteomes; UP000051819; Unassembled WGS sequence.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:InterPro.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR   CDD; cd00430; PLPDE_III_AR; 1.
DR   Gene3D; 3.20.20.10; Alanine 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   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR600821-50};
KW   Reference proteome {ECO:0000313|Proteomes:UP000051819}.
FT   DOMAIN          209..336
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   BINDING         101
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         278
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         5
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   350 AA;  36447 MW;  36D51C511E2B6792 CRC64;
     MAVLKADAFG HGAIARSVLE AGATSIGVTS IDEAIALRVD GISAPILSWL NPVDADFEAA
     VLADIDLAVP SAALLQAVAR TAAGAGRRAR VHLHIDVGMA RDGAPAGEWA ALCGIAREFE
     HLGWIRVVGV MGHMSCADQP EHPQNQRERL VFANAVRTAL RRGLAPTVTH LAATAATLTG
     VGAGFGMHRI GAGLFGIDPS GTSAELRPAL SLTTHVVAAR EVAPGTGIGY GLDHIADRRT
     HLALLPIGYG DGLPRGASER ADVFVRGRRR PLVGRFSMDM VVADTGDDAV APGEPVLVFG
     PGGDGEPTVA EWALWSGTIE HEIVTRIGTR VARIHRTTGA YRGQRGAVRA
//
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