ID A0A372ERW8_9RHOB Unreviewed; 371 AA.
AC A0A372ERW8;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE RecName: Full=alanine racemase {ECO:0000256|ARBA:ARBA00013089};
DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089};
GN ORFNames=DZK27_14740 {ECO:0000313|EMBL:RFP86341.1};
OS Rhodobacteraceae bacterium 63075.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae.
OX NCBI_TaxID=2301226 {ECO:0000313|EMBL:RFP86341.1, ECO:0000313|Proteomes:UP000264392};
RN [1] {ECO:0000313|Proteomes:UP000264392}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=63075 {ECO:0000313|Proteomes:UP000264392};
RA Han S.;
RT "Wenzhouxiangella salilacus sp. nov., a novel bacterium isolated from a
RT saline lake in Xinjiang Province, China.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-alanine = D-alanine; Xref=Rhea:RHEA:20249,
CC ChEBI:CHEBI:57416, ChEBI:CHEBI:57972; EC=5.1.1.1;
CC Evidence={ECO:0000256|ARBA:ARBA00000316};
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:RFP86341.1}.
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DR EMBL; QVMW01000019; RFP86341.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A372ERW8; -.
DR OrthoDB; 9813814at2; -.
DR Proteomes; UP000264392; Unassembled WGS sequence.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
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 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 3: Inferred from homology;
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:UP000264392}.
FT DOMAIN 243..371
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT BINDING 138
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 312
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 371 AA; 39840 MW; 29F7AA7B6A37B391 CRC64;
MSRDIYPDSW CEIHLGRIAC NLDLALGLVP PGRKLCAVLK ADAYGHGIEK VVPLMMAGGI
DCIGITSNAE AFAVRDAGFD GPMIRVRAAS TGEIDAALEA RVEEQVASLE VAERLVALRD
AGHPVRAHLA LNSLGMSRDG LEISTEEGRA TCLSIVKRLA GNIVGICTHF PSNTPEDLRS
SADLFRDHVA WVFENSPLER SEVLVHAGSS LTLVSGEPVE TDMYRCGAIL YGILNPELGF
RTTMDLKARV VSVGEYPAGA TVGYDKGFRL GSDRRLACLS IGYANGFRRG RTPDAAVMLA
GRAAPVLGKV SMNTIVADVS DIDGIAPGDE AMVFGGIADT RDSLETTERQ FRTIMADLYA
DWGLRNARVY R
//
