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Database: UniProt
Entry: R4YXD0_9ACTN
LinkDB: R4YXD0_9ACTN
Original site: R4YXD0_9ACTN 
ID   R4YXD0_9ACTN            Unreviewed;       238 AA.
AC   R4YXD0;
DT   24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT   24-JUL-2013, sequence version 1.
DT   27-MAR-2024, entry version 37.
DE   RecName: Full=Alanine racemase N-terminal domain-containing protein {ECO:0000259|Pfam:PF01168};
GN   ORFNames=BN381_140003 {ECO:0000313|EMBL:CCM62838.1};
OS   Candidatus Microthrix parvicella RN1.
OC   Bacteria; Actinomycetota; Acidimicrobiia; Acidimicrobiales;
OC   Microthrixaceae; Microthrix.
OX   NCBI_TaxID=1229780 {ECO:0000313|EMBL:CCM62838.1, ECO:0000313|Proteomes:UP000018291};
RN   [1] {ECO:0000313|EMBL:CCM62838.1, ECO:0000313|Proteomes:UP000018291}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=RN1 {ECO:0000313|EMBL:CCM62838.1,
RC   ECO:0000313|Proteomes:UP000018291};
RX   PubMed=23446830; DOI=10.1038/ismej.2013.6;
RA   Jon McIlroy S., Kristiansen R., Albertsen M., Michael Karst S.,
RA   Rossetti S., Lund Nielsen J., Tandoi V., James Seviour R., Nielsen P.H.;
RT   "Metabolic model for the filamentous 'Candidatus Microthrix parvicella'
RT   based on genomic and metagenomic analyses.";
RL   ISME J. 7:1161-1172(2013).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|PIRSR:PIRSR004848-1};
CC   -!- SIMILARITY: Belongs to the pyridoxal phosphate-binding protein
CC       YggS/PROSC family. {ECO:0000256|RuleBase:RU004514}.
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:CCM62838.1}.
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DR   EMBL; CANL01000006; CCM62838.1; -; Genomic_DNA.
DR   RefSeq; WP_012224639.1; NZ_HG422565.1.
DR   AlphaFoldDB; R4YXD0; -.
DR   STRING; 1229780.BN381_140003; -.
DR   GeneID; 78313239; -.
DR   eggNOG; COG0325; Bacteria.
DR   HOGENOM; CLU_059988_0_1_11; -.
DR   OrthoDB; 9804072at2; -.
DR   Proteomes; UP000018291; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR011078; PyrdxlP_homeostasis.
DR   NCBIfam; TIGR00044; YggS family pyridoxal phosphate-dependent enzyme; 1.
DR   PANTHER; PTHR10146; PROLINE SYNTHETASE CO-TRANSCRIBED BACTERIAL HOMOLOG PROTEIN; 1.
DR   PANTHER; PTHR10146:SF14; PYRIDOXAL PHOSPHATE HOMEOSTASIS PROTEIN; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   PIRSF; PIRSF004848; YBL036c_PLPDEIII; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS01211; UPF0001; 1.
PE   3: Inferred from homology;
KW   Pyridoxal phosphate {ECO:0000256|PIRSR:PIRSR004848-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018291}.
FT   DOMAIN          30..228
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   MOD_RES         46
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004848-1"
SQ   SEQUENCE   238 AA;  25122 MW;  8478637CC621256C CRC64;
     MNELANVSPP PDVRVLSEQI AERSALVRER LDRTAGREVR VVAVSKSHPP STAWAAALAG
     HREFGENYAQ ELVGKAGFLA ERGIEVRWHM IGPVQSNKVK VLAPVLGWWH TIDRSKLVRT
     IARWSPEGTV MIQRNLSGDP NKAGCTADEV EPLVAEATEA GLDVVGLMGV ATEGSPQLAA
     AEFASLVAQA DALALRERCI GMSGDLDVAL AAGATTVRLG SMLFGSRPGS ANGGPSRA
//
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