ID A0A0N1ALG8_9SPHN Unreviewed; 358 AA.
AC A0A0N1ALG8;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE RecName: Full=alanine racemase {ECO:0000256|ARBA:ARBA00013089};
DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089};
GN ORFNames=IP65_04975 {ECO:0000313|EMBL:KPF55463.1};
OS Novosphingobium sp. AAP1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1523413 {ECO:0000313|EMBL:KPF55463.1, ECO:0000313|Proteomes:UP000037880};
RN [1] {ECO:0000313|EMBL:KPF55463.1, ECO:0000313|Proteomes:UP000037880}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=AAP1 {ECO:0000313|EMBL:KPF55463.1,
RC ECO:0000313|Proteomes:UP000037880};
RA Zeng Y., Feng F., Liu Y., Koblizek M.;
RT "Novel Diversity of Limnic Aerobic Anoxygenic Phototrophic Bacteria as
RT Revealed by High-throughput Strain Identification and Genome Sequencing.";
RL Submitted (AUG-2015) 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:KPF55463.1}.
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DR EMBL; LJHO01000002; KPF55463.1; -; Genomic_DNA.
DR RefSeq; WP_028657482.1; NZ_LJHO01000002.1.
DR AlphaFoldDB; A0A0N1ALG8; -.
DR STRING; 1523413.IP65_04975; -.
DR PATRIC; fig|1523413.3.peg.1701; -.
DR OrthoDB; 9813814at2; -.
DR Proteomes; UP000037880; 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:UP000037880}.
FT DOMAIN 233..354
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 302
FT /ligand="substrate"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 44
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 358 AA; 37720 MW; 1710B78AF0A661CE CRC64;
MSVFSSVPLP PAALRLAFDA TALAGNWRAL DRLSGAASAG AAVKADAYGL GAARVVPVLA
QAGCRDWFVA HWCEVPDLLP HVPAASIHVL HGPMNAADVA YARATGVTPV LNSLAQVQRW
LTAGGGRCDL MVDTGINRLG LPMADLGDPG LAALDIDCCI SHLASADEDV AQNAQQLARF
QAVRTQIKAR RYSLANSAGI ALGAPWHADV TRPGIAIYGG IVRSELAGVI APVARPQAAV
IQRRQLHPGD HVGYNATFTA DRPVAAAVVA LGYADGYLRT WSGRGEFLWQ GKTLPVIGRI
SMDMTIVDAT DAPALVEGDW LDVAYNLPEA AKISGLSQYE LLTLLGRRFL RDKACLAP
//