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Database: UniProt/TrEMBL
Entry: F8GVI8_CUPNN
LinkDB: F8GVI8_CUPNN
Original site: F8GVI8_CUPNN 
ID   F8GVI8_CUPNN            Unreviewed;       372 AA.
AC   F8GVI8;
DT   21-SEP-2011, integrated into UniProtKB/TrEMBL.
DT   21-SEP-2011, sequence version 1.
DT   27-MAR-2024, entry version 73.
DE   SubName: Full=Alanine racemase Alr {ECO:0000313|EMBL:AEI81547.1};
DE            EC=5.1.1.1 {ECO:0000313|EMBL:AEI81547.1};
GN   Name=alr {ECO:0000313|EMBL:AEI81547.1};
GN   OrderedLocusNames=CNE_BB1p01200 {ECO:0000313|EMBL:AEI81547.1};
OS   Cupriavidus necator (strain ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453
OS   / N-1) (Ralstonia eutropha).
OG   Plasmid pBB1 {ECO:0000313|EMBL:AEI81547.1,
OG   ECO:0000313|Proteomes:UP000006798}.
OC   Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC   Burkholderiaceae; Cupriavidus.
OX   NCBI_TaxID=1042878 {ECO:0000313|EMBL:AEI81547.1, ECO:0000313|Proteomes:UP000006798};
RN   [1] {ECO:0000313|EMBL:AEI81547.1, ECO:0000313|Proteomes:UP000006798}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 43291 / DSM 13513 / CCUG 52238 / LMG 8453 / N-1
RC   {ECO:0000313|Proteomes:UP000006798};
RC   PLASMID=pBB1 {ECO:0000313|EMBL:AEI81547.1,
RC   ECO:0000313|Proteomes:UP000006798};
RX   PubMed=21742890; DOI=10.1128/JB.05660-11;
RA   Poehlein A., Kusian B., Friedrich B., Daniel R., Bowien B.;
RT   "Complete genome sequence of the type strain Cupriavidus necator N-1.";
RL   J. Bacteriol. 193:5017-5017(2011).
CC   -!- COFACTOR:
CC       Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC         Evidence={ECO:0000256|ARBA:ARBA00001933,
CC         ECO:0000256|PIRSR:PIRSR600821-50};
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DR   EMBL; CP002879; AEI81547.1; -; Genomic_DNA.
DR   RefSeq; WP_013958605.1; NC_015727.1.
DR   AlphaFoldDB; F8GVI8; -.
DR   KEGG; cnc:CNE_BB1p01200; -.
DR   HOGENOM; CLU_028393_2_2_4; -.
DR   Proteomes; UP000006798; Plasmid pBB1.
DR   GO; GO:0008784; F:alanine racemase activity; IEA:UniProtKB-EC.
DR   GO; GO:0006522; P:alanine metabolic process; IEA:InterPro.
DR   Gene3D; 3.20.20.10; Alanine 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; 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.
PE   4: Predicted;
KW   Isomerase {ECO:0000256|ARBA:ARBA00023235, ECO:0000313|EMBL:AEI81547.1};
KW   Plasmid {ECO:0000313|EMBL:AEI81547.1};
KW   Pyridoxal phosphate {ECO:0000256|ARBA:ARBA00022898,
KW   ECO:0000256|PIRSR:PIRSR600821-50}.
FT   DOMAIN          240..368
FT                   /note="Alanine racemase C-terminal"
FT                   /evidence="ECO:0000259|SMART:SM01005"
FT   BINDING         135
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT   BINDING         309
FT                   /ligand="substrate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-52"
FT   MOD_RES         36
FT                   /note="N6-(pyridoxal phosphate)lysine"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR600821-50"
SQ   SEQUENCE   372 AA;  40216 MW;  78854A975A97561F CRC64;
     MENNAWVEVD LGKFEANVRG IQTRIGDRAE MCAVMKADAC GHGIALLVPT LVALGVSSIG
     IARNDEARQV RQAGFTGRLL RVRAATLAEI EDGLPYGLEE IVGNLDYARH IDALVHRYRR
     VARVHLELNS GGMSRNGFDL DSQPEREKCL AAAALPHLRV VGIMTHFPVQ EVSDVERGLA
     RFRDEAAWLI ASASMVRSQI QLHCANSFTT LEVPAAHLDM VRTGAILFGC LPAYPDFQPI
     ASLKSRVASV NAYAAGNTVA YDRTLCLSRD SRLANIPVGY ADGYRRALSN RGQALIRGRV
     YPVVGRVTMN TLMVDVTESP DILPGDEVVL FGTQGGSRID VASIEAAAGT IYPDLCVGWG
     NSVTRVAVPA NH
//
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