ID Q20XT3_RHOPB Unreviewed; 1183 AA.
AC Q20XT3;
DT 18-APR-2006, integrated into UniProtKB/TrEMBL.
DT 18-APR-2006, sequence version 1.
DT 24-JAN-2024, entry version 103.
DE SubName: Full=Allophanate hydrolase subunit 2 {ECO:0000313|EMBL:ABD90053.1};
GN OrderedLocusNames=RPC_4531 {ECO:0000313|EMBL:ABD90053.1};
OS Rhodopseudomonas palustris (strain BisB18).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Rhodopseudomonas.
OX NCBI_TaxID=316056 {ECO:0000313|EMBL:ABD90053.1};
RN [1] {ECO:0000313|EMBL:ABD90053.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=BisB18 {ECO:0000313|EMBL:ABD90053.1};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Chain P., Malfatti S., Shin M., Vergez L., Schmutz J., Larimer F., Land M.,
RA Hauser L., Pelletier D.A., Kyrpides N., Anderson I., Oda Y., Harwood C.S.,
RA Richardson P.;
RT "Complete sequence of Rhodopseudomonas palustris BisB18.";
RL Submitted (MAR-2006) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; CP000301; ABD90053.1; -; Genomic_DNA.
DR AlphaFoldDB; Q20XT3; -.
DR STRING; 316056.RPC_4531; -.
DR KEGG; rpc:RPC_4531; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG1984; Bacteria.
DR eggNOG; COG2049; Bacteria.
DR HOGENOM; CLU_002162_0_1_5; -.
DR OMA; TLQMWNR; -.
DR OrthoDB; 9763189at2; -.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
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; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR014084; Urea_COase.
DR NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR NCBIfam; TIGR02712; urea_carbox; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 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};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABD90053.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..444
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1103..1181
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1183 AA; 127885 MW; F15494B946B503EA CRC64;
MFDKVLIANR GEIASRIGKT LRRIGIASVA VYSDADRFTR AVLDADQAVR VGASPAAESY
LNIDAIIKAC RETGAQAVHP GYGFLSENRG FAERLASHGI VFIGPRPEHL DAFGLKHKAR
ELAQHSNVPL LPGSGLLETI DEAMREAERI GFPLMLKSTA GGGGIGMQLC HDADTLRERF
ATVQRTAKAS FGDARVYLER FVAEARHIEV QIFGDGQGKV IALGERDCSL QRRNQKVIEE
TPAPGLSDEL RTRLHRAAVA LGESVAYQSA GTVEFIYDVA REDFYFLEVN TRLQVEHPVT
EAVFGVDLVE WMVRQAAGDS PLANYTPRPP QGAAIEVRLY AENPNAGFRP SAGRLTDVEF
PDGVRVDGWI ETGVEVTPFY DPMLAKLIVH ADSRDQAIDK LRDALQQSRV AGIETNLDYL
RAIAGSELFR SGRVATNVLA SFAFAPRTID VLAPGAQSGL QELPGRLHLW HVGVPPSGPM
DERSFRLANI IVGNPEVTAA LELTVNGPTL RFNTDAVIGL AGAHMLAKLD GVAIAHHAPV
AVKAGQTLQI GKIDGAGQRC YLAVRGGFDA PQILGSRAVF MLGAFGGHST GALKPGDVLH
IVAESDALAA PRAATPDEIP PFTRAWQIGV IYGPHGAPDF FRDDDIATLF STDYEVHFNS
ARTGVRLIGP KPQWARADGG EAGLHPSNIH DNAYAVGSLD FTGDMPIILG PDGPSLGGFV
CPAVVARDEL WKIGQLKPGD KVRFVPLPRD DDPVAGPTVL AGPRELGSAI VAGRDDGAMP
VVYRRAGDDN LLVEYGPMEL DIALRLRVQL LADAVAAAKL PGLIDLTPGI RSLQIHYDGA
TLSRRKLLDA LAAIEGELPA VDAMRVPSRV VHLPLSWNDP QAVKAMHKYQ ELVRPDAPWC
PSNIDFIRRI NGLDDEAAVQ RIVFDASYLV LGLGDVYLGA PVATPVDPRH RLVTTKYNPA
RTWTPENAVG IGGAYMCIYG MEGPGGYQLF GRTIQMWNSW RSTPEFTPGH PWLLRFFDQI
RFFPVSASEL LEAREAFPHG QYPLRIEETV FSYADYAKGL ARDQDSIAAF KQRQQAAFEA
ERQRWKQLRL DAVQDDESAG AEAAPDDIPD GATGVFSEVP GNVWKILVDE GAMVAAGDTL
AIIESMKMEI SVPAPVAGRL ASIRIKPGQT LRAGDVVAVI AEG
//