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Database: UniProt
Entry: L0KU33_MESAW
LinkDB: L0KU33_MESAW
Original site: L0KU33_MESAW 
ID   L0KU33_MESAW            Unreviewed;       608 AA.
AC   L0KU33;
DT   06-MAR-2013, integrated into UniProtKB/TrEMBL.
DT   06-MAR-2013, sequence version 1.
DT   27-MAR-2024, entry version 49.
DE   SubName: Full=Putative amino acid racemase {ECO:0000313|EMBL:AGB48195.1};
GN   OrderedLocusNames=Mesau_05974 {ECO:0000313|EMBL:AGB48195.1};
OS   Mesorhizobium australicum (strain HAMBI 3006 / LMG 24608 / WSM2073).
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC   Phyllobacteriaceae; Mesorhizobium.
OX   NCBI_TaxID=754035 {ECO:0000313|EMBL:AGB48195.1, ECO:0000313|Proteomes:UP000010998};
RN   [1] {ECO:0000313|Proteomes:UP000010998}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=LMG 24608 / HAMBI 3006 / WSM2073
RC   {ECO:0000313|Proteomes:UP000010998};
RA   Lucas S., Han J., Lapidus A., Cheng J.-F., Goodwin L., Pitluck S.,
RA   Peters L., Gu W., Detter J.C., Han C., Tapia R., Land M., Hauser L.,
RA   Kyrpides N., Ivanova N., Pagani I., Reeve W.G., Howieson J.G., Tiwari R.P.,
RA   O'Hara G.W., Atkins C.A., Ronson C.W., Nandasena K.G., Woyke T.;
RT   "Complete sequence of Mesorhizobium australicum WSM2073.";
RL   Submitted (FEB-2012) to the EMBL/GenBank/DDBJ databases.
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933};
CC   -!- SIMILARITY: Belongs to the arginase family. {ECO:0000256|PROSITE-
CC       ProRule:PRU00742}.
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DR   EMBL; CP003358; AGB48195.1; -; Genomic_DNA.
DR   RefSeq; WP_015319240.1; NC_019973.1.
DR   AlphaFoldDB; L0KU33; -.
DR   STRING; 754035.Mesau_05974; -.
DR   KEGG; mam:Mesau_05974; -.
DR   eggNOG; COG0010; Bacteria.
DR   eggNOG; COG3457; Bacteria.
DR   HOGENOM; CLU_448931_0_0_5; -.
DR   OrthoDB; 504078at2; -.
DR   Proteomes; UP000010998; Chromosome.
DR   GO; GO:0047661; F:amino-acid racemase activity; IEA:UniProt.
DR   GO; GO:0016813; F:hydrolase activity, acting on carbon-nitrogen (but not peptide) bonds, in linear amidines; IEA:UniProt.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   CDD; cd06815; PLPDE_III_AR_like_1; 1.
DR   Gene3D; 3.20.20.10; Alanine racemase; 1.
DR   Gene3D; 3.40.800.10; Ureohydrolase domain; 1.
DR   InterPro; IPR001608; Ala_racemase_N.
DR   InterPro; IPR029066; PLP-binding_barrel.
DR   InterPro; IPR006035; Ureohydrolase.
DR   InterPro; IPR023696; Ureohydrolase_dom_sf.
DR   PANTHER; PTHR30511; ALANINE RACEMASE; 1.
DR   PANTHER; PTHR30511:SF3; LYSINE RACEMASE; 1.
DR   Pfam; PF01168; Ala_racemase_N; 1.
DR   Pfam; PF00491; Arginase; 1.
DR   PRINTS; PR00116; ARGINASE.
DR   SUPFAM; SSF52768; Arginase/deacetylase; 1.
DR   SUPFAM; SSF51419; PLP-binding barrel; 1.
DR   PROSITE; PS51409; ARGINASE_2; 1.
PE   3: Inferred from homology;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235};
KW   Reference proteome {ECO:0000313|Proteomes:UP000010998}.
FT   DOMAIN          8..224
FT                   /note="Alanine racemase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF01168"
SQ   SEQUENCE   608 AA;  65175 MW;  C69E8B6B684DBD9F CRC64;
     MSGPQVAIDL GRIERNARTV VDRCALSGIK VFGVTKGTCG MPQVARAMLR GGVSGIAESR
     FENIRRLRDS GISAPIMLLR SPPMARVEEV VRTVDVSLQS ELTIIREISR IAERMGRVHN
     IMLMIDLGDL REGIWPNDLI PTVERILDMK GVRIAGIGTN LGCFGAIMPT EENLGQLVAH
     AYKTERLSGK SLDFISGGAS SSLPLLLEGK LPAGINNLRI GEAILQGGVE TFRDVPWAEL
     EPDACRLTSD VIEVKLKPSR PIGTSGYDAF GNQPVFPDEG DRLRAIANIG REDVLVEGLA
     PIAKGIRVLG ASSDHLLLDV QDADPPLAVG DRVAFRMSYG AMLLAMTSEY VEKAPMHDVA
     DFSGRKMVSI SAEAEAARIL AREATGARLE AMNFDVVELA DVDRPPSGLI RFAAGADRRI
     AHKALTATAR ATHSFGLIWI DSIAALMPED EDGIDLPEVS VLARSLGLDH KPGALQPQLS
     PENVVVIGLR HADPAEVRVL KDSRVSAFTM TDIDAMGMRD LMHEAIRIAT SGTQGFHVSY
     SPTATEFAGW AAGSGGLTVR ETHQAMEAIA LSGGLLSMDV SGLSTDLEPR IGSDTVNFVM
     SAFGKRIL
//
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