ID A0A0P7WEW9_9SPHN Unreviewed; 347 AA.
AC A0A0P7WEW9;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 24-JAN-2024, entry version 30.
DE RecName: Full=alanine racemase {ECO:0000256|ARBA:ARBA00013089};
DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089};
GN Name=alr {ECO:0000313|EMBL:KPP88755.1};
GN ORFNames=HLUCCO15_11070 {ECO:0000313|EMBL:KPP88755.1};
OS Erythrobacteraceae bacterium HL-111.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Erythrobacteraceae.
OX NCBI_TaxID=1666908 {ECO:0000313|EMBL:KPP88755.1, ECO:0000313|Proteomes:UP000050295};
RN [1] {ECO:0000313|EMBL:KPP88755.1, ECO:0000313|Proteomes:UP000050295}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HL-111 {ECO:0000313|EMBL:KPP88755.1};
RA Nelson W.C., Romine M.F., Lindemann S.R.;
RT "Identification and resolution of microdiversity through metagenomic
RT sequencing of parallel consortia.";
RL Submitted (SEP-2015) 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 -!- SIMILARITY: Belongs to the alanine racemase family.
CC {ECO:0000256|ARBA:ARBA00007880}.
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:KPP88755.1}.
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DR EMBL; LJSW01000026; KPP88755.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A0P7WEW9; -.
DR PATRIC; fig|1666908.3.peg.930; -.
DR Proteomes; UP000050295; 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; 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.
PE 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW ECO:0000256|PIRSR:PIRSR600821-50}.
FT DOMAIN 229..347
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 298
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 40
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 347 AA; 35935 MW; DC3AB7073FC52981 CRC64;
MGADPPAPTL RLDIDTQALA ANWRAMDALS GRAAAGAAVK ADCYGLGADT CVPVLREAGC
RHFFVAHWSE VAGVARHVPA GEIAVLHGPV TRAEADYARA VGAVPVINSP EQARTWSAAG
GGPCHLMVDT GINRLGVALR DLADPAIAAL EIDVLMSHLA CADEDSPMNP RQLEAFRAAC
GQVPHRRASL ANSAGIALGP DYAFDLTRPG LALYGGVPRA ELAPIVRPVA RLAAKLIQCR
TIEPGESVGY NAAFTAPAAM RVGTVSLGYA DGFLRARGPG GAFASAGRGL PILGKVSMDM
VVVDLAAAPD LGPGDWVEVP FDLVDAAQQT ILSQYELLTL LGARLKS
//
