GenomeNet

Database: UniProt/TrEMBL
Entry: Q0AQD6_MARMM
LinkDB: Q0AQD6_MARMM
Original site: Q0AQD6_MARMM 
ID   Q0AQD6_MARMM            Unreviewed;       366 AA.
AC   Q0AQD6;
DT   17-OCT-2006, integrated into UniProtKB/TrEMBL.
DT   17-OCT-2006, sequence version 1.
DT   24-JAN-2024, entry version 112.
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   OrderedLocusNames=Mmar10_1208 {ECO:0000313|EMBL:ABI65501.1};
OS   Maricaulis maris (strain MCS10).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Maricaulales; Maricaulaceae;
OC   Maricaulis.
OX   NCBI_TaxID=394221 {ECO:0000313|EMBL:ABI65501.1, ECO:0000313|Proteomes:UP000001964};
RN   [1] {ECO:0000313|EMBL:ABI65501.1, ECO:0000313|Proteomes:UP000001964}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=MCS10 {ECO:0000313|EMBL:ABI65501.1,
RC   ECO:0000313|Proteomes:UP000001964};
RG   US DOE Joint Genome Institute;
RA   Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA   Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA   Saunders E., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA   Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Viollier P.,
RA   Stephens C., Richardson P.;
RT   "Complete sequence of Maricaulis maris MCS10.";
RL   Submitted (AUG-2006) 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|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; CP000449; ABI65501.1; -; Genomic_DNA.
DR   RefSeq; WP_011643148.1; NC_008347.1.
DR   AlphaFoldDB; Q0AQD6; -.
DR   STRING; 394221.Mmar10_1208; -.
DR   KEGG; mmr:Mmar10_1208; -.
DR   eggNOG; COG0787; Bacteria.
DR   HOGENOM; CLU_028393_1_1_5; -.
DR   OMA; WEILCGF; -.
DR   OrthoDB; 9813814at2; -.
DR   UniPathway; UPA00042; UER00497.
DR   Proteomes; UP000001964; 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}; Reference proteome {ECO:0000313|Proteomes:UP000001964}.
FT   DOMAIN          242..365
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   ACT_SITE        45
FT                   /note="Proton acceptor; specific for D-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   ACT_SITE        263
FT                   /note="Proton acceptor; specific for L-alanine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201"
FT   BINDING         141
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         311
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         45
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_01201,
FT                   ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   366 AA;  39396 MW;  C8488A266E50C1CC CRC64;
     MSDTGTSSRR AHPAPRLIID LAAIKRNYAA LQTLAPTASV GAVVKANGYG LGAAQVVPAL
     ADAGCRCFYV AHTSEAREAR EALAGRPADI FVFNGFWPSE LAELRQLSLF PVINDLQQLE
     DLRALAPDLP CAIHFDTGMS RLGLDAAETE ALLADPARID ALDVRQIMSH LACSDDPDHP
     LNEQQRQRFE RIRHALPGIP ASLSNSTGTL LGQAYHFDML RPGLALFSGM PAPGQASPFE
     PVVAIDAPIL QIRTLQPGDT VGYGACWTAD RPRRVATVAA GYADGLLRAF GNGGYGRIGE
     TQVPILGRVS MDLICVDIDA VEEPVRPGDP VRFLGPDIEN MADSAATISY EFLVRLGIRF
     DRSYLR
//
DBGET integrated database retrieval system