ID A8HW84_AZOC5 Unreviewed; 1176 AA.
AC A8HW84;
DT 04-DEC-2007, integrated into UniProtKB/TrEMBL.
DT 04-DEC-2007, sequence version 1.
DT 27-MAR-2024, entry version 84.
DE SubName: Full=Allophanate hydrolase subunit 2 {ECO:0000313|EMBL:BAF90400.1};
GN OrderedLocusNames=AZC_4402 {ECO:0000313|EMBL:BAF90400.1};
OS Azorhizobium caulinodans (strain ATCC 43989 / DSM 5975 / JCM 20966 / LMG
OS 6465 / NBRC 14845 / NCIMB 13405 / ORS 571).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Xanthobacteraceae; Azorhizobium.
OX NCBI_TaxID=438753 {ECO:0000313|EMBL:BAF90400.1, ECO:0000313|Proteomes:UP000000270};
RN [1] {ECO:0000313|EMBL:BAF90400.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=17720818; DOI=10.1128/AEM.01514-07;
RA Suzuki S., Aono T., Lee KB., Suzuki T., Liu CT., Miwa H., Wakao S., Iki T.,
RA Oyaizu H.;
RT "Rhizobial factors required for stem nodule maturation and maintenance in
RT Sesbania rostrata-Azorhizobium caulinodans ORS571 symbiosis.";
RL Appl. Environ. Microbiol. 73:6650-6659(2007).
RN [2] {ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RA Lee K.B., Backer P.D., Aono T., Liu C.T., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T., Ussery D., Vereecke D., Gevers D., Holsters M., Oyaizu H.;
RT "Complete genome sequence of the nitrogen-fixing bacterium Azorhizobium
RT caulinodans ORS571.";
RL Submitted (APR-2007) to the EMBL/GenBank/DDBJ databases.
RN [3] {ECO:0000313|EMBL:BAF90400.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=18522759; DOI=10.1186/1471-2164-9-271;
RA Lee KB., Backer P.D., Aono T., Liu CT., Suzuki S., Suzuki T., Kaneko T.,
RA Yamada M., Tabata S., Kupfer D.M., Najar F.Z., Wiley G.B., Roe B.,
RA Binnewies T.T., Ussery D.W., D'Haeze W., Herder J.D., Gevers D.,
RA Vereecke D., Holsters M., Oyaizu H.;
RT "The genome of the versatile nitrogen fixer Azorhizobium caulinodans
RT ORS571.";
RL BMC Genomics 9:271-271(2008).
RN [4] {ECO:0000313|EMBL:BAF90400.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=19542345; DOI=10.1128/AEM.00398-09;
RA Tsukada S., Aono T., Akiba N., Lee KB., Liu CT., Toyazaki H., Oyaizu H.;
RT "Comparative genome-wide transcriptional profiling of Azorhizobium
RT caulinodans ORS571 grown under free-living and symbiotic conditions.";
RL Appl. Environ. Microbiol. 75:5037-5046(2009).
RN [5] {ECO:0000313|EMBL:BAF90400.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=20382809; DOI=10.1128/AEM.00238-10;
RA Akiba N., Aono T., Toyazaki H., Sato S., Oyaizu H.;
RT "phrR-like gene praR of Azorhizobium caulinodans ORS571 is essential for
RT symbiosis with Sesbania rostrata and is involved in expression of reb
RT genes.";
RL Appl. Environ. Microbiol. 76:3475-3485(2010).
RN [6] {ECO:0000313|EMBL:BAF90400.1, ECO:0000313|Proteomes:UP000000270}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43989 / DSM 5975 / JCM 20966 / LMG 6465 / NBRC 14845 /
RC NCIMB 13405 / ORS 571 {ECO:0000313|Proteomes:UP000000270};
RX PubMed=21571889; DOI=10.1128/AEM.02327-10;
RA Liu CT., Lee KB., Wang YS., Peng MH., Lee KT., Suzuki S., Suzuki T.,
RA Oyaizu H.;
RT "Involvement of the azorhizobial chromosome partition gene (parA) in the
RT onset of bacteroid differentiation during Sesbania rostrata stem nodule
RT development.";
RL Appl. Environ. Microbiol. 77:4371-4382(2011).
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; AP009384; BAF90400.1; -; Genomic_DNA.
DR RefSeq; WP_012172922.1; NC_009937.1.
DR AlphaFoldDB; A8HW84; -.
DR STRING; 438753.AZC_4402; -.
DR KEGG; azc:AZC_4402; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG1984; Bacteria.
DR eggNOG; COG2049; Bacteria.
DR HOGENOM; CLU_002162_3_1_5; -.
DR Proteomes; UP000000270; Chromosome.
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; IPR006594; LisH.
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.
DR PROSITE; PS50896; LISH; 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:BAF90400.1};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000000270}.
FT DOMAIN 1..443
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 1095..1173
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1176 AA; 125327 MW; E2F1D1DFED294C5C CRC64;
MFRTVLIANR GEIASRIGRT LRAMGIRVVA VYSDADRFTR GVLEADEAHR LGPAPAAQSY
LDVEAVIAAA KASGAEAVHP GYGFLSENVA FAERLAAEGI AFIGPKPKHL RAFGLKHTAR
ELAQASGVPL LPGTGLIDSV DEALAAAEAI SYPVMLKSTA GGGGIGMQLC ADAQELAAAF
ERVQRTARAS FGDARVYLER FVAEARHVEV QIFGNGQGRV VALGERDCSL QRRNQKVIEE
TPAPLLPDAV RTRLHAAAVA LGESVGYASA GTVEFIYDPA REEFYFLEVN TRLQVEHPVT
EAVFGIDLVE WMVRQAAGED PIPATPLTPK GAAIEARVYA EIPHANFQPS AGLLTEVAFP
AGVRVDGWVE TGSEVTPFYD PMLAKVIVTG ADRAAALAAL KAALAETRLS GIETNLAYLR
AIAASDLFAS GKVATTALKD FAFTPRSIEV LTPGAQSSLQ ELPGRLHLWH VGVPPSGPMD
AYSFRRANAL VRNHPDTAAL ELTVNGPTLR FHTAAEVALS GAHMPATLDG ASVPHDAAFA
VKAGQVLAIG AISGAGQRTY LAVRGGFDAP EVLGSRATFA LGAFGGHATG TLKGGDVLHL
GTAPEAATVP PPSAPLTREW EIGVVYGPHG APDFFQPEDI ADLFEAAYEV HFNSARTGVR
LIGPTPRWAR TDGGEAGLHP SNLHDNAYAI GAIDFTGDMP IILGPDGPSL GGFVCPAVIA
RDEQWKMGQL KPGDTVRFRP AVRPQDAIAG PEVFSAPEAG SPIVARRTDG PVEVVYRRQG
DDNLLVEFGD MRLDIALRLR AHLMAQAVEE AKLPGLIDLT PGIRSLQLHY DGTSLTRARL
LGALQEIEAS LPAAEDVVVP SRTVHLPLSW DDPDAQLAMR KYQELVRPNA PWCPSNIEFI
RRINGLPDEQ AVKDIVFDAR YLVLGLGDVY LGAPVATPID PRHRLVTTKY NPARTWTPEN
AVGIGGAYMC IYGMEGPGGY QLFGRTIQMW NTWRATPAFA PGTPWLLRFF DQIRFFPVSH
QELTEARAAF PHGAYPVRIE EGSFSYADYA AGLKRNAAAI SAFKTRQQAA FEAEKARWKA
EGLDSFVSDE GGPALAPDAI PDGCFGVSAN VPGNVWKVLV EPGAPVAAGE TIAIIESMKM
EIAITAHAAG RLREVRAVPG RTVRTGDVVA VLEAVA
//