ID F5SZL3_9GAMM Unreviewed; 471 AA.
AC F5SZL3;
DT 27-JUL-2011, integrated into UniProtKB/TrEMBL.
DT 27-JUL-2011, sequence version 1.
DT 24-JAN-2024, entry version 42.
DE SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:EGL54440.1};
GN ORFNames=MAMP_01054 {ECO:0000313|EMBL:EGL54440.1};
OS Methylophaga aminisulfidivorans MP.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Thiotrichales;
OC Piscirickettsiaceae; Methylophaga.
OX NCBI_TaxID=1026882 {ECO:0000313|EMBL:EGL54440.1, ECO:0000313|Proteomes:UP000003544};
RN [1] {ECO:0000313|EMBL:EGL54440.1, ECO:0000313|Proteomes:UP000003544}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MP(T) {ECO:0000313|Proteomes:UP000003544};
RX PubMed=21685284; DOI=10.1128/JB.05403-11;
RA Han G.H., Kim W., Chun J., Kim S.W.;
RT "Draft genome sequence of Methylophaga aminisulfidivorans MP T.";
RL J. Bacteriol. 193:4265-4265(2011).
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:EGL54440.1}.
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DR EMBL; AFIG01000001; EGL54440.1; -; Genomic_DNA.
DR RefSeq; WP_007144326.1; NZ_AFIG01000001.1.
DR AlphaFoldDB; F5SZL3; -.
DR STRING; 1026882.MAMP_01054; -.
DR eggNOG; COG0439; Bacteria.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000003544; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR PANTHER; PTHR48095:SF1; BIOTIN CARBOXYLASE; 1.
DR PANTHER; PTHR48095; PYRUVATE CARBOXYLASE SUBUNIT A; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000003544}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 119..315
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 471 AA; 52273 MW; 25A00ABBEB234D19 CRC64;
MLKKVLIANR GEIAVRIVRA CAEMGIRSVA IYTEPDRYAL HVKRADESYS LGDDPLAGYL
DPLRIVNLAV ETGCDAIHPG YGFLSENAEF ARLCEKNNIT FVGPKSSVIE KMGDKTAARD
SMRDAGVPIT PGSDGNLADL DEALALAEEV GYPVMIKATS GGGGRGIRRC DSANELRQQY
PRVISEATKA FGSAEVFLEK CIVNPRHIEV QILADSEGNV VHLYERDCSI QRRNQKLIEI
APSPQLTPEQ RDYVGGLAVK AAQAVNYENA GTVEFLLTGN EVYFMEMNTR VQVEHTITEQ
ITGIDIVREQ LRIASGLPLS YRQQDIAYRG YALQFRINAE DPKNDFLPSF GRITHYYAPG
GPGVRVDTAI YTGYEIPPYF DSMCLKLVVW ALDWEDAISR GQRALDDMRL HGIKTTENYY
KQILNHPDFR SGHFDTSFVP NHPELLNYSN KRRPSAVALA LATAIAAHAG W
//
