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}.
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; 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
//