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Database: UniProt
Entry: A8UQU8_9AQUI
LinkDB: A8UQU8_9AQUI
Original site: A8UQU8_9AQUI 
ID   A8UQU8_9AQUI            Unreviewed;       348 AA.
AC   A8UQU8;
DT   15-JAN-2008, integrated into UniProtKB/TrEMBL.
DT   15-JAN-2008, sequence version 1.
DT   24-JAN-2024, entry version 87.
DE   RecName: Full=Alanine racemase {ECO:0000256|HAMAP-Rule:MF_01201};
DE            EC=5.1.1.1 {ECO:0000256|HAMAP-Rule:MF_01201};
GN   ORFNames=HG1285_02548 {ECO:0000313|EMBL:EDP76450.1};
OS   Hydrogenivirga sp. 128-5-R1-1.
OC   Bacteria; Aquificota; Aquificae; Aquificales; Aquificaceae; Hydrogenivirga.
OX   NCBI_TaxID=392423 {ECO:0000313|EMBL:EDP76450.1, ECO:0000313|Proteomes:UP000005981};
RN   [1] {ECO:0000313|EMBL:EDP76450.1, ECO:0000313|Proteomes:UP000005981}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=128-5-R1-1 {ECO:0000313|EMBL:EDP76450.1,
RC   ECO:0000313|Proteomes:UP000005981};
RA   Reysenbach A.-L., Ferriera S., Johnson J., Kravitz S., Beeson K.,
RA   Sutton G., Rogers Y.-H., Friedman R., Frazier M., Venter J.C.;
RL   Submitted (OCT-2007) to the EMBL/GenBank/DDBJ databases.
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|HAMAP-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. {ECO:0000256|HAMAP-
CC       Rule:MF_01201}.
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:EDP76450.1}.
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DR   EMBL; ABHJ01000001; EDP76450.1; -; Genomic_DNA.
DR   AlphaFoldDB; A8UQU8; -.
DR   PATRIC; fig|392423.7.peg.3565; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000005981; Unassembled WGS sequence.
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; IPR000595; cNMP-bd_dom.
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.
DR   PROSITE; PS50042; CNMP_BINDING_3; 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}; Reference proteome {ECO:0000313|Proteomes:UP000005981}.
FT   DOMAIN          269..325
FT                   /note="Cyclic nucleotide-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50042"
FT   ACT_SITE        43
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        246
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         136
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         294
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         43
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   348 AA;  38925 MW;  B0751B21BEAF05A8 CRC64;
     MVEGYCGALL GCRSVLRIKR SAVEENVREL FRFGGKKLIA VIKSDAYGIG VKYVAPILRE
     LPEVESFAVA CVEEGVLLRE MGIKREVLIL GGILPEELEA VKEYGLTPVV SDIEHLKIIG
     NEDIKFHVKY DTGMGRLGFV DEFVDDPRVV GIMSHLSTPA DEEFSRKQIE RFEAIVRRYS
     RKIKVHLESS AGVIYRVPYT THIRVGLAIY GEKPLKEYPL RLRPAVSIRA RVLSLKTLPA
     GHPISYGRTF VTEREMRIGV IAFGYADGLM KSLSNRGYLL YEGNKLPIVG NITMDMTIVD
     VGTANVRVGD WVTVVSEERT FGELAREAGT IPYELMCNVS SRVKREVT
//
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