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
//