ID   LAMA_EMENI              Reviewed;        1241 AA.
AC   P38095; C8VUT6; Q5BEZ3;
DT   01-OCT-1994, integrated into UniProtKB/Swiss-Prot.
DT   26-MAY-2009, sequence version 2.
DT   24-JAN-2024, entry version 112.
DE   RecName: Full=Putative urea carboxylase;
DE            EC=6.3.4.6;
DE   AltName: Full=Lactam utilization protein lamA;
DE   AltName: Full=Urea amidolyase;
GN   Name=lamA; ORFNames=AN0887;
OS   Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 /
OS   M139) (Aspergillus nidulans).
OC   Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC   Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC   Aspergillus subgen. Nidulantes.
OX   NCBI_TaxID=227321;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=16372000; DOI=10.1038/nature04341;
RA   Galagan J.E., Calvo S.E., Cuomo C., Ma L.-J., Wortman J.R., Batzoglou S.,
RA   Lee S.-I., Bastuerkmen M., Spevak C.C., Clutterbuck J., Kapitonov V.,
RA   Jurka J., Scazzocchio C., Farman M.L., Butler J., Purcell S., Harris S.,
RA   Braus G.H., Draht O., Busch S., D'Enfert C., Bouchier C., Goldman G.H.,
RA   Bell-Pedersen D., Griffiths-Jones S., Doonan J.H., Yu J., Vienken K.,
RA   Pain A., Freitag M., Selker E.U., Archer D.B., Penalva M.A., Oakley B.R.,
RA   Momany M., Tanaka T., Kumagai T., Asai K., Machida M., Nierman W.C.,
RA   Denning D.W., Caddick M.X., Hynes M., Paoletti M., Fischer R., Miller B.L.,
RA   Dyer P.S., Sachs M.S., Osmani S.A., Birren B.W.;
RT   "Sequencing of Aspergillus nidulans and comparative analysis with A.
RT   fumigatus and A. oryzae.";
RL   Nature 438:1105-1115(2005).
RN   [2]
RP   GENOME REANNOTATION.
RC   STRAIN=FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139;
RX   PubMed=19146970; DOI=10.1016/j.fgb.2008.12.003;
RA   Wortman J.R., Gilsenan J.M., Joardar V., Deegan J., Clutterbuck J.,
RA   Andersen M.R., Archer D., Bencina M., Braus G., Coutinho P., von Dohren H.,
RA   Doonan J., Driessen A.J., Durek P., Espeso E., Fekete E., Flipphi M.,
RA   Estrada C.G., Geysens S., Goldman G., de Groot P.W., Hansen K.,
RA   Harris S.D., Heinekamp T., Helmstaedt K., Henrissat B., Hofmann G.,
RA   Homan T., Horio T., Horiuchi H., James S., Jones M., Karaffa L.,
RA   Karanyi Z., Kato M., Keller N., Kelly D.E., Kiel J.A., Kim J.M.,
RA   van der Klei I.J., Klis F.M., Kovalchuk A., Krasevec N., Kubicek C.P.,
RA   Liu B., Maccabe A., Meyer V., Mirabito P., Miskei M., Mos M., Mullins J.,
RA   Nelson D.R., Nielsen J., Oakley B.R., Osmani S.A., Pakula T., Paszewski A.,
RA   Paulsen I., Pilsyk S., Pocsi I., Punt P.J., Ram A.F., Ren Q., Robellet X.,
RA   Robson G., Seiboth B., van Solingen P., Specht T., Sun J.,
RA   Taheri-Talesh N., Takeshita N., Ussery D., vanKuyk P.A., Visser H.,
RA   van de Vondervoort P.J., de Vries R.P., Walton J., Xiang X., Xiong Y.,
RA   Zeng A.P., Brandt B.W., Cornell M.J., van den Hondel C.A., Visser J.,
RA   Oliver S.G., Turner G.;
RT   "The 2008 update of the Aspergillus nidulans genome annotation: a community
RT   effort.";
RL   Fungal Genet. Biol. 46:S2-13(2009).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-103.
RC   STRAIN=biA1 niiA4;
RX   PubMed=1729609; DOI=10.1128/mcb.12.1.337-346.1992;
RA   Richardson I.B., Katz M.E., Hynes M.J.;
RT   "Molecular characterization of the lam locus and sequences involved in
RT   regulation by the AmdR protein of Aspergillus nidulans.";
RL   Mol. Cell. Biol. 12:337-346(1992).
RN   [4]
RP   FUNCTION.
RX   PubMed=2670678; DOI=10.1016/0378-1119(89)90324-7;
RA   Katz M.E., Hynes M.J.;
RT   "Gene function identified by interspecific transformation.";
RL   Gene 78:167-171(1989).
RN   [5]
RP   FUNCTION, AND INDUCTION.
RX   PubMed=2670667; DOI=10.1093/genetics/122.2.331;
RA   Katz M.E., Hynes M.J.;
RT   "Characterization of the amdR-controlled lamA and lamB genes of Aspergillus
RT   nidulans.";
RL   Genetics 122:331-339(1989).
CC   -!- FUNCTION: Involved in the utilization of lactams. Required for the
CC       conversion of exogenous 2-pyrrolidinone (gamma-butyrolactam) to
CC       endogenous gamma-amino-n-butyrate (GABA). {ECO:0000269|PubMed:2670667,
CC       ECO:0000269|PubMed:2670678}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + hydrogencarbonate + urea = ADP + H(+) + phosphate +
CC         urea-1-carboxylate; Xref=Rhea:RHEA:20896, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:15832, ChEBI:CHEBI:16199, ChEBI:CHEBI:17544,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:456216; EC=6.3.4.6;
CC   -!- COFACTOR:
CC       Name=biotin; Xref=ChEBI:CHEBI:57586; Evidence={ECO:0000250};
CC   -!- INDUCTION: By beta-alanine. {ECO:0000269|PubMed:2670667}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAA33312.1; Type=Erroneous translation; Note=Wrong choice of frame.; Evidence={ECO:0000305};
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DR   EMBL; AACD01000014; EAA65916.1; -; Genomic_DNA.
DR   EMBL; M77283; AAA33312.1; ALT_SEQ; Genomic_DNA.
DR   EMBL; BN001308; CBF88588.1; -; Genomic_DNA.
DR   PIR; A42064; A42064.
DR   RefSeq; XP_658491.1; XM_653399.1.
DR   AlphaFoldDB; P38095; -.
DR   SMR; P38095; -.
DR   STRING; 227321.P38095; -.
DR   EnsemblFungi; CBF88588; CBF88588; ANIA_00887.
DR   GeneID; 2876661; -.
DR   KEGG; ani:AN0887.2; -.
DR   eggNOG; KOG0238; Eukaryota.
DR   HOGENOM; CLU_002162_0_1_1; -.
DR   InParanoid; P38095; -.
DR   OMA; TLQMWNR; -.
DR   OrthoDB; 313213at2759; -.
DR   Proteomes; UP000000560; Chromosome VIII.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0004847; F:urea carboxylase activity; IEA:UniProtKB-EC.
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; IPR001882; Biotin_BS.
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   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; PS00188; BIOTIN; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR   PROSITE; PS00866; CPSASE_1; 1.
DR   PROSITE; PS00867; CPSASE_2; 1.
PE   2: Evidence at transcript level;
KW   ATP-binding; Biotin; Hydrolase; Ligase; Nucleotide-binding;
KW   Reference proteome.
FT   CHAIN           1..1241
FT                   /note="Putative urea carboxylase"
FT                   /id="PRO_0000084354"
FT   DOMAIN          3..459
FT                   /note="Biotin carboxylation"
FT   DOMAIN          121..321
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00409"
FT   DOMAIN          1159..1239
FT                   /note="Biotinyl-binding"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU01066"
FT   BINDING         117
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   BINDING         201
FT                   /ligand="ATP"
FT                   /ligand_id="ChEBI:CHEBI:30616"
FT                   /evidence="ECO:0000250"
FT   MOD_RES         1202
FT                   /note="N6-biotinyllysine"
FT                   /evidence="ECO:0000250, ECO:0000255|PROSITE-
FT                   ProRule:PRU01066"
SQ   SEQUENCE   1241 AA;  135753 MW;  0534958F6957FA0F CRC64;
     MEALKTLLIA NRGEIAVRVL KTAKKLNIRT IAVYTEPDAA STHVHLADEA ILLSGPPSKA
     YIDGDQIIDI AKRKGADAII PGYGFLSENS NFARDVASAG LAFVGPSPES IEAFGLKHTA
     RELATKAGVP IVPGSQGLVT SEDEAVKIAQ SLGFPVMLKA TAGGGGMGLL TCNTEKEVRE
     SFQTVQSRGE ALFKNAGLFI ERYYPSSHHI EVQVFGNGQG KAISIGEREC SIQRRHQKVI
     EECPSPFVTR NPELRKGLCD AAVRLAESID YGSAGTIEYL VDDESGKFFF LEMNTRLQVE
     HGITELCYGV DLVELMLRQA DAQLSGRKGL EAEFLSSIPV GAPQGFAIEA RVYAENPVRD
     FAPCPGILQD VDWKETTGSR IDTWVYRGIK VSANYDPLLA KVMYHASSRQ KAIEGLRDIL
     TGSRICGPPT NLGFLAEILA NKDFNAGNTL TKFLNNFEYN LAAIDVISGG AYTLIQDWPG
     RPTVGRGFCH SGPMDSVAFR IANALVGNPV GLEGLEITLS GPELRFLGPA VISLCGAPID
     AKLDEAPVPM WSRVKVSAGQ RLKIGKTTGG GCRAYLAVLG GFPNIAEWFG SKATAPMVGV
     GGYQGRQLTS GDYLTISAQI PESDNELSLP EHLIPQYPDS WELMSMPGPY DEGYLAPESI
     DMLYNAEWTI SHNAARGGIR LLGPKPTWAR PDGGEGGAHP SNLIECGYAI GSINWTGDDP
     VIFPQDAPDL GGFVSSHTIV KADLWKLGQV KAGDKLKFRA TSLKDTLLAR NELERFISDI
     VQCCQKGEDF GSITPLASSL PPAMSSSTRV SGIVHQIPEK GNQPLVSYRQ AGDDYLLIDY
     GVGAFDLNHR YRVTALKKVL SEAAGDISVS NGLINLVGCG NYLPKALMIY YDGTKIPQQK
     LIDYLCTIET QLGDLSRAKV PSRRFKLPLT FESKRQTDAI KRYMETQRPY ASYLPDNIDF
     VARNNAFTRA ELENIYLTAS FMVITVGFFT ALPIALPVDP RQRMNCPKMN PSRVFTPAGQ
     VSWGGSCLAI YTVDSPGGYQ MNGMTIPGVD ILGTKRGYAP EKPWLFEDFD QITFYKVTEE
     EYERQLALFQ SGRYEYEWEV VEFDMAEHNR LLKETKEEVK AIRARQRKAQ AEMDLLEKEL
     LERWAKEKAE RGVSMDTVEE LLKDPEITVI EAPLNANVWK VEVKEGDKLD KDQVVVILEA
     MKLEIAVRAE SAAAGAVVEK ILAQPGKSIE AGKPLMLVRR G
//