ID G0AI07_COLFT Unreviewed; 264 AA.
AC G0AI07;
DT 19-OCT-2011, integrated into UniProtKB/TrEMBL.
DT 19-OCT-2011, sequence version 1.
DT 27-MAR-2024, entry version 59.
DE RecName: Full=Pyridoxal phosphate homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
DE Short=PLP homeostasis protein {ECO:0000256|HAMAP-Rule:MF_02087};
GN OrderedLocusNames=CFU_0756 {ECO:0000313|EMBL:AEK60590.1};
OS Collimonas fungivorans (strain Ter331).
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Oxalobacteraceae; Collimonas.
OX NCBI_TaxID=1005048 {ECO:0000313|EMBL:AEK60590.1, ECO:0000313|Proteomes:UP000008392};
RN [1] {ECO:0000313|EMBL:AEK60590.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60590.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=15305924; DOI=10.1111/j.1462-2920.2004.00673.x;
RA Leveau J.H., Gerards S., de Boer W., van Veen J.A.;
RT "Phylogeny-function analysis of (meta)genomic libraries: screening for
RT expression of ribosomal RNA genes by large-insert library fluorescent in
RT situ hybridization (LIL-FISH).";
RL Environ. Microbiol. 6:990-998(2004).
RN [2] {ECO:0000313|EMBL:AEK60590.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60590.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=16457898; DOI=10.1016/j.mimet.2005.12.010;
RA Leveau J.H., Gerards S., Fritsche K., Zondag G., van Veen J.A.;
RT "Genomic flank-sequencing of plasposon insertion sites for rapid
RT identification of functional genes.";
RL J. Microbiol. Methods 66:276-285(2006).
RN [3] {ECO:0000313|EMBL:AEK60590.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60590.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=18671744; DOI=10.1111/j.1574-6941.2008.00547.x;
RA Fritsche K., de Boer W., Gerards S., van den Berg M., van Veen J.A.,
RA Leveau J.H.;
RT "Identification and characterization of genes underlying chitinolysis in
RT Collimonas fungivorans Ter331.";
RL FEMS Microbiol. Ecol. 66:123-135(2008).
RN [4] {ECO:0000313|EMBL:AEK60590.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60590.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=19638176; DOI=10.1111/j.1462-2920.2009.02010.x;
RA Leveau J.H., Uroz S., de Boer W.;
RT "The bacterial genus Collimonas: mycophagy, weathering and other adaptive
RT solutions to life in oligotrophic soil environments.";
RL Environ. Microbiol. 12:281-292(2010).
RN [5] {ECO:0000313|EMBL:AEK60590.1, ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|EMBL:AEK60590.1,
RC ECO:0000313|Proteomes:UP000008392};
RX PubMed=21614084; DOI=10.1038/ismej.2011.29;
RA Mela F., Fritsche K., de Boer W., van Veen J.A., de Graaff L.H.,
RA van den Berg M., Leveau J.H.;
RT "Dual transcriptional profiling of a bacterial/fungal confrontation:
RT Collimonas fungivorans versus Aspergillus niger.";
RL ISME J. 5:1494-1504(2011).
RN [6] {ECO:0000313|Proteomes:UP000008392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ter331 {ECO:0000313|Proteomes:UP000008392};
RA Leveau J.H.;
RT "Complete sequence of Collimonas fungivorans Ter331.";
RL Submitted (MAY-2011) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Pyridoxal 5'-phosphate (PLP)-binding protein, which is
CC involved in PLP homeostasis. {ECO:0000256|HAMAP-Rule:MF_02087}.
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|HAMAP-Rule:MF_02087,
CC ECO:0000256|RuleBase:RU004514}.
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DR EMBL; CP002745; AEK60590.1; -; Genomic_DNA.
DR AlphaFoldDB; G0AI07; -.
DR STRING; 1005048.CFU_0756; -.
DR KEGG; cfu:CFU_0756; -.
DR eggNOG; COG0325; Bacteria.
DR HOGENOM; CLU_059988_0_1_4; -.
DR Proteomes; UP000008392; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR CDD; cd06824; PLPDE_III_Yggs_like; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR HAMAP; MF_02087; PLP_homeostasis; 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|HAMAP-Rule:MF_02087,
KW ECO:0000256|PIRSR:PIRSR004848-1};
KW Reference proteome {ECO:0000313|Proteomes:UP000008392}.
FT DOMAIN 43..258
FT /note="Alanine racemase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF01168"
FT MOD_RES 51
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_02087,
FT ECO:0000256|PIRSR:PIRSR004848-1"
SQ SEQUENCE 264 AA; 28746 MW; 8CD3BA10AB597D19 CRC64;
MQISSSLRQF SNSPIMSLMS HKLQAVHSSI HATAITASRR PDSVALLAVS KTFGADAVLE
AVAAGQRAFG ENYLQEALTK MAEVELKLAL KSGEGDDVLL EWHFIGPIQS NKTRAIAEHF
DWVHTVDREK IAQRLSQQRP PQLAPLNICL QVNISGEASK SGLAPAEVKD VARAIAGLPG
LKLRGLMAIP EPTDDLEKQH AAFRRTRQLL EQLQQDPDMQ QAGQQLDTLS MGMSADMAAA
IEEGATIVRV GSAIFGQRER NHDK
//
