ID   A0A087QGM9_APTFO        Unreviewed;       245 AA.
AC   A0A087QGM9;
DT   29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT   29-OCT-2014, sequence version 1.
DT   24-JAN-2024, entry version 23.
DE   SubName: Full=Proline synthase co-transcribed bacterial protein {ECO:0000313|EMBL:KFM00383.1};
DE   Flags: Fragment;
GN   ORFNames=AS27_08352 {ECO:0000313|EMBL:KFM00383.1};
OS   Aptenodytes forsteri (Emperor penguin).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Archelosauria; Archosauria; Dinosauria; Saurischia; Theropoda;
OC   Coelurosauria; Aves; Neognathae; Sphenisciformes; Spheniscidae;
OC   Aptenodytes.
OX   NCBI_TaxID=9233 {ECO:0000313|EMBL:KFM00383.1, ECO:0000313|Proteomes:UP000053286};
RN   [1] {ECO:0000313|EMBL:KFM00383.1, ECO:0000313|Proteomes:UP000053286}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=BGI_AS27 {ECO:0000313|EMBL:KFM00383.1};
RA   Zhang G., Li C.;
RT   "Genome evolution of avian class.";
RL   Submitted (APR-2014) to the EMBL/GenBank/DDBJ databases.
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}.
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DR   EMBL; KL225562; KFM00383.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A087QGM9; -.
DR   STRING; 9233.A0A087QGM9; -.
DR   Proteomes; UP000053286; Unassembled WGS sequence.
DR   GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR   CDD; cd06822; PLPDE_III_YBL036c_euk; 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|PIRSR:PIRSR004848-1};
KW   Reference proteome {ECO:0000313|Proteomes:UP000053286}.
FT   DOMAIN          8..218
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
FT   REGION          223..245
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         15
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR004848-1"
FT   NON_TER         1
FT                   /evidence="ECO:0000313|EMBL:KFM00383.1"
FT   NON_TER         245
FT                   /evidence="ECO:0000313|EMBL:KFM00383.1"
SQ   SEQUENCE   245 AA;  26635 MW;  418193C8FFE4E18D CRC64;
     QGLPAVQPRL VAVSKTKPAE MVIDAYSHGQ RSFGENYVQE LLEKASDSRI LSSCPEIKWH
     FIGHLQKNNV NKLIAVPNLF MLETVDSVKL ADRVNSSWQK KGSSQKLKVM VQVNTSGEDS
     KHGLPPGDTT AAVEHVINKC PSLEFVGLMT IGSIGHDLSK GPNPDFQMLL SLRQEVCEKL
     NLPVETVELS MGMSTDFQHA VKVGSTNVRI GSTIFGERDY SNKAVGGKAP AETKGETETL
     AVQGH
//