ID A0A0G0Z1B2_9BACT Unreviewed; 376 AA.
AC A0A0G0Z1B2;
DT 22-JUL-2015, integrated into UniProtKB/TrEMBL.
DT 22-JUL-2015, sequence version 1.
DT 24-JAN-2024, entry version 37.
DE SubName: Full=Alanine racemase {ECO:0000313|EMBL:KKS42570.1};
GN ORFNames=UV02_C0011G0018 {ECO:0000313|EMBL:KKS42570.1};
OS Candidatus Kuenenbacteria bacterium GW2011_GWA2_42_15.
OC Bacteria; Candidatus Kuenenbacteria.
OX NCBI_TaxID=1618677 {ECO:0000313|EMBL:KKS42570.1, ECO:0000313|Proteomes:UP000034516};
RN [1] {ECO:0000313|EMBL:KKS42570.1, ECO:0000313|Proteomes:UP000034516}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Brown C.T., Hug L.A., Thomas B.C., Sharon I., Castelle C.J., Singh A.,
RA Wilkins M.J., Williams K.H., Banfield J.F.;
RT "rRNA introns, odd ribosomes, and small enigmatic genomes across a large
RT radiation of phyla.";
RL Nature 0:0-0(2015).
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:KKS42570.1}.
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DR EMBL; LCCW01000011; KKS42570.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0G0Z1B2; -.
DR PATRIC; fig|1618677.3.peg.223; -.
DR Proteomes; UP000034516; 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}.
FT DOMAIN 247..375
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT BINDING 131
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 316
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 376 AA; 41230 MW; 9D032A406936878C CRC64;
MKQKTWVEVS KKALQINIAE LKTIIGEDVF ILAIIKGNAY GAGIETTVSA TKSIVAWFGV
DSLDEANLAR KNCQNPILIL GYVANNDAAE VVKNQFSVIV YNYDLAVALS RKATAENPAK
IHIKVDTGLV RLGLWPEDAI ILVKKISKLP NIIVEGMCTH FAKLINENNV EIYSAQLKKF
IFVVDSLANL GIQPKIMHAA SSMSAVLYKA THLNMVRIGS ALYGLWGRES LLKFMHEKNN
EFNLCPALSW KTTVVNIKKI PLNTGVGYLH SEIVSRDTTV AVLGAGCYDG IDKRYAKVGY
VLINGKRAKI LGGITMNMCM VDATGIENIK IGDEAVLIGR SGQEEITVYD FAKVINTSTH
EVISRINPLL SRILVP
//
