ID A0A261FBJ4_9BIFI Unreviewed; 508 AA.
AC A0A261FBJ4;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 25.
DE SubName: Full=Alanine racemase {ECO:0000313|EMBL:OZG56405.1};
GN ORFNames=AEAE_0893 {ECO:0000313|EMBL:OZG56405.1};
OS Aeriscardovia aeriphila.
OC Bacteria; Actinomycetota; Actinomycetes; Bifidobacteriales;
OC Bifidobacteriaceae; Aeriscardovia.
OX NCBI_TaxID=218139 {ECO:0000313|EMBL:OZG56405.1, ECO:0000313|Proteomes:UP000228976};
RN [1] {ECO:0000313|EMBL:OZG56405.1, ECO:0000313|Proteomes:UP000228976}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 21773 {ECO:0000313|EMBL:OZG56405.1,
RC ECO:0000313|Proteomes:UP000228976};
RX PubMed=28764658; DOI=10.1186/s12864-017-3955-4;
RA Lugli G.A., Milani C., Turroni F., Duranti S., Mancabelli L.,
RA Mangifesta M., Ferrario C., Modesto M., Mattarelli P., Jiri K.,
RA van Sinderen D., Ventura M.;
RT "Comparative genomic and phylogenomic analyses of the Bifidobacteriaceae
RT family.";
RL BMC Genomics 18:568-568(2017).
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:OZG56405.1}.
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DR EMBL; MWWU01000002; OZG56405.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A261FBJ4; -.
DR Proteomes; UP000228976; 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; IPR020622; Ala_racemase_pyridoxalP-BS.
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.
DR PROSITE; PS00395; ALANINE_RACEMASE; 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:UP000228976}.
FT DOMAIN 309..485
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT BINDING 184
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 400
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 83
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 508 AA; 55086 MW; 7E7F9D5AC5ECAC44 CRC64;
MRTQQAQDSG DTDSFMHEEM HSDNLSHTFH GERALDFSPV DNPYPQATTR YPAQIIVDLA
AIRDNVRSLR ERNNNAQVLT VIKANGYGHG FLPTALAALA GGSTWFGAAQ PHDLLILREA
GIGADRAHMI TWMWTATEDL AAIARADIDF SVSTLSQIRQ LAQLAHEIGQ RVRIHVACDT
GFGRNGFTPQ ALPEALDLLK KLASTDPADE VADKPLLLVG QFSHLAVADA PDDPLSVAST
DEQINTYQWF SEQLDQVGLT PSVRHLANTA ASLTRPEISL DMVRPGIGIY GYSADPAMGL
GLAYGLKPAL RLQAQLATVR TLPANHAIGY GRTYITQHES LLAIVPVGYS DGIPRSASGF
NERGWQHTEH QGGPVLLGTV RLRNGSEAGV IAHVAGRVCM DQFMLALSAE TVEIRDHSGN
LVELSASDYQ SLISQIREGD TVLLFGPGRG SEYGEPNLEE WAASANTITY EILTRLGSRF
PRIYENAREV LTDADLAMLE HAGIALGK
//
