ID A0A074LHE9_9BACT Unreviewed; 385 AA.
AC A0A074LHE9;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Alanine racemase {ECO:0000313|EMBL:KEO73207.1};
GN ORFNames=EL17_12690 {ECO:0000313|EMBL:KEO73207.1};
OS Anditalea andensis.
OC Bacteria; Bacteroidota; Cytophagia; Cytophagales; Cytophagaceae; Anditalea.
OX NCBI_TaxID=1048983 {ECO:0000313|EMBL:KEO73207.1, ECO:0000313|Proteomes:UP000027821};
RN [1] {ECO:0000313|EMBL:KEO73207.1, ECO:0000313|Proteomes:UP000027821}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LY1 {ECO:0000313|EMBL:KEO73207.1,
RC ECO:0000313|Proteomes:UP000027821};
RA Yang L., Wei S., Tay Q.X.M.;
RT "Characterization and application of a salt tolerant electro-active
RT bacterium.";
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|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:KEO73207.1}.
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DR EMBL; JMIH01000022; KEO73207.1; -; Genomic_DNA.
DR RefSeq; WP_035074932.1; NZ_JMIH01000022.1.
DR AlphaFoldDB; A0A074LHE9; -.
DR STRING; 1048983.EL17_12690; -.
DR eggNOG; COG0787; Bacteria.
DR OrthoDB; 9801978at2; -.
DR Proteomes; UP000027821; 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:UP000027821}.
FT DOMAIN 256..384
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT BINDING 135
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 325
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 36
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 385 AA; 43507 MW; B93753756D28A601 CRC64;
MQGTSYIEIS RSAYRKNLKF MRSQVGEKPI LSAVIKGNAY GHGIENMVKI AEEAGIRHFS
TYSADEAYRA YKACKKESQI MIMGMATDEQ LDWVIENGID IFMFESDRLE KAIDIAKNKG
KKARIHIEVE TGFNRTGFDW DHREALSAIL RANLDYLSLE GLCTHYAGAE SIGNYVRVHR
QIEKYHQFKN YFSEQGLPFS IYHTACSAAA LSYPETIMDM VRIGIALYGF WPSQETYLGK
YKDLKAYPGN NPLQRLLSWK SQVMSIKHVK RGEFIGYGTS FMAPRDMTIA LVPVGYCHGF
SRKLSNLGKV LVQGKILTVV GTVTMNSIAV DATDLKHIER GEPVVIIGKQ KKQELTVASF
GESSNQVNYE LLTRLPLDIE RRIVP
//
