ID A0A0G3I3X1_LIBAF Unreviewed; 370 AA.
AC A0A0G3I3X1;
DT 16-SEP-2015, integrated into UniProtKB/TrEMBL.
DT 16-SEP-2015, sequence version 1.
DT 24-JAN-2024, entry version 35.
DE RecName: Full=Alanine racemase {ECO:0000256|ARBA:ARBA00013089, ECO:0000256|HAMAP-Rule:MF_01201};
DE EC=5.1.1.1 {ECO:0000256|ARBA:ARBA00013089, ECO:0000256|HAMAP-Rule:MF_01201};
GN ORFNames=G293_01340 {ECO:0000313|EMBL:AKK19900.1};
OS Candidatus Liberibacter africanus PTSAPSY.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Rhizobiaceae; Liberibacter.
OX NCBI_TaxID=1277257 {ECO:0000313|EMBL:AKK19900.1, ECO:0000313|Proteomes:UP000035503};
RN [1] {ECO:0000313|Proteomes:UP000035503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTSAPSY {ECO:0000313|Proteomes:UP000035503};
RA Lin H., Pietersen G., Sahota P., Lou B., Han S., Read D.A., Civerolo E.L.,
RA Gupta G.;
RT "Complete genome sequence of 'Candidatus Liberibacter africanus, bacterium
RT associated with citrus huanglongbing'.";
RL Submitted (DEC-2012) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:AKK19900.1, ECO:0000313|Proteomes:UP000035503}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=PTSAPSY {ECO:0000313|EMBL:AKK19900.1,
RC ECO:0000313|Proteomes:UP000035503};
RX PubMed=26184931;
RA Lin H., Pietersen G., Han C., Read D.A., Lou B., Gupta G., Civerolo E.L.;
RT "Complete Genome Sequence of 'Candidatus Liberibacter africanus,' a
RT Bacterium Associated with Citrus Huanglongbing.";
RL Genome Announc. 3:e00733-15(2015).
CC -!- FUNCTION: Catalyzes the interconversion of L-alanine and D-alanine. May
CC also act on other amino acids. {ECO:0000256|HAMAP-Rule:MF_01201}.
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, ECO:0000256|HAMAP-
CC Rule:MF_01201};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000256|ARBA:ARBA00001933,
CC ECO:0000256|HAMAP-Rule:MF_01201, ECO:0000256|PIRSR:PIRSR600821-50};
CC -!- PATHWAY: Amino-acid biosynthesis; D-alanine biosynthesis; D-alanine
CC from L-alanine: step 1/1. {ECO:0000256|HAMAP-Rule:MF_01201}.
CC -!- SIMILARITY: Belongs to the alanine racemase family.
CC {ECO:0000256|ARBA:ARBA00007880, ECO:0000256|HAMAP-Rule:MF_01201}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; CP004021; AKK19900.1; -; Genomic_DNA.
DR RefSeq; WP_047263964.1; NZ_CP004021.1.
DR AlphaFoldDB; A0A0G3I3X1; -.
DR STRING; 1277257.G293_01340; -.
DR KEGG; lau:G293_01340; -.
DR PATRIC; fig|1277257.4.peg.293; -.
DR OrthoDB; 9813814at2; -.
DR UniPathway; UPA00042; UER00497.
DR Proteomes; UP000035503; Chromosome.
DR GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:UniProtKB-UniRule.
DR GO; GO:0030632; P:D-alanine biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd00430; PLPDE_III_AR; 1.
DR Gene3D; 3.20.20.10; Alanine racemase; 1.
DR HAMAP; MF_01201; Ala_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 3: Inferred from homology;
KW Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000256|HAMAP-Rule:MF_01201};
KW Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898, ECO:0000256|HAMAP-
KW Rule:MF_01201}.
FT DOMAIN 235..370
FT /note="Alanine racemase C-terminal"
FT /evidence="ECO:0000259|SMART:SM01005"
FT ACT_SITE 37
FT /note="Proton acceptor; specific for D-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT ACT_SITE 256
FT /note="Proton acceptor; specific for L-alanine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT BINDING 134
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT BINDING 315
FT /ligand="substrate"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-52"
FT MOD_RES 37
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT ECO:0000256|PIRSR:PIRSR600821-50"
SQ SEQUENCE 370 AA; 40430 MW; FADCEAEBC6A4F49E CRC64;
MHSNEFLKLT IDLTALKNNW HSVNQLSGSA RTAAVVKDDA YGLGLEKIAI ALYNAGAQDF
FVTDVAEGVK LRSYLPKAKI FVLYGINPGE EKHLFNANLI PVISSISQLS FYGKLISSGV
CHPYALQVDT GFNRLGLSLE EALDFAQNYL NKKSDNLSLI MSHLACADDP KSHVNSVQLK
RFRTLVTYYK GVEASLVSSA GILLGSDYHF QLTRPGISLY GGTHTINKSH PMETVVTAEA
RIIQIRKSLA GEIISYGGGK KLTRNSLIAV ASIGYADGYP LTMSRLDSKN KPFLFSGGEG
FVKGYTAPVL GKITMDMTMF DITDSPGIKV GDYIQVFGSH IKLDDVAVAS GTTNYDLLVR
IGKRYAKFYR
//
