ID A0A194RNM8_PAPMA Unreviewed; 1458 AA.
AC A0A194RNM8;
DT 05-OCT-2016, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2016, sequence version 1.
DT 08-NOV-2023, entry version 30.
DE RecName: Full=hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00012655};
DE EC=2.5.1.61 {ECO:0000256|ARBA:ARBA00012655};
DE AltName: Full=Hydroxymethylbilane synthase {ECO:0000256|ARBA:ARBA00033064};
GN ORFNames=RR48_07109 {ECO:0000313|EMBL:KPJ17621.1};
OS Papilio machaon (Old World swallowtail butterfly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Lepidoptera; Glossata; Ditrysia; Papilionoidea;
OC Papilionidae; Papilioninae; Papilio.
OX NCBI_TaxID=76193 {ECO:0000313|EMBL:KPJ17621.1, ECO:0000313|Proteomes:UP000053240};
RN [1] {ECO:0000313|EMBL:KPJ17621.1, ECO:0000313|Proteomes:UP000053240}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Ya'a_city_454_Pm {ECO:0000313|EMBL:KPJ17621.1};
RC TISSUE=Whole body {ECO:0000313|EMBL:KPJ17621.1};
RX PubMed=26354079; DOI=10.1038/ncomms9212;
RA Li X., Fan D., Zhang W., Liu G., Zhang L., Zhao L., Fang X., Chen L.,
RA Dong Y., Chen Y., Ding Y., Zhao R., Feng M., Zhu Y., Feng Y., Jiang X.,
RA Zhu D., Xiang H., Feng X., Li S., Wang J., Zhang G., Kronforst M.R.,
RA Wang W.;
RT "Outbred genome sequencing and CRISPR/Cas9 gene editing in butterflies.";
RL Nat. Commun. 6:8212-8212(2015).
CC -!- COFACTOR:
CC Name=dipyrromethane; Xref=ChEBI:CHEBI:60342;
CC Evidence={ECO:0000256|ARBA:ARBA00001916};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; coproporphyrinogen-III from 5-aminolevulinate: step 2/4.
CC {ECO:0000256|ARBA:ARBA00004735}.
CC -!- SIMILARITY: Belongs to the HMBS family.
CC {ECO:0000256|ARBA:ARBA00005638}.
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DR EMBL; KQ460124; KPJ17621.1; -; Genomic_DNA.
DR STRING; 76193.A0A194RNM8; -.
DR InParanoid; A0A194RNM8; -.
DR UniPathway; UPA00251; UER00319.
DR Proteomes; UP000053240; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0004418; F:hydroxymethylbilane synthase activity; IEA:UniProtKB-EC.
DR GO; GO:0004672; F:protein kinase activity; IEA:InterPro.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR CDD; cd13645; PBP2_HuPBGD_like; 1.
DR Gene3D; 3.40.190.10; Periplasmic binding protein-like II; 2.
DR Gene3D; 3.30.160.40; Porphobilinogen deaminase, C-terminal domain; 1.
DR Gene3D; 1.10.510.10; Transferase(Phosphotransferase) domain 1; 2.
DR HAMAP; MF_00260; Porphobil_deam; 1.
DR InterPro; IPR000860; HemC.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR022419; Porphobilin_deaminase_cofac_BS.
DR InterPro; IPR022417; Porphobilin_deaminase_N.
DR InterPro; IPR022418; Porphobilinogen_deaminase_C.
DR InterPro; IPR036803; Porphobilinogen_deaminase_C_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR NCBIfam; TIGR00212; hemC; 1.
DR PANTHER; PTHR11557; PORPHOBILINOGEN DEAMINASE; 1.
DR PANTHER; PTHR11557:SF0; PORPHOBILINOGEN DEAMINASE; 1.
DR Pfam; PF00069; Pkinase; 1.
DR Pfam; PF01379; Porphobil_deam; 1.
DR Pfam; PF03900; Porphobil_deamC; 1.
DR PRINTS; PR00151; PORPHBDMNASE.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF53850; Periplasmic binding protein-like II; 1.
DR SUPFAM; SSF54782; Porphobilinogen deaminase (hydroxymethylbilane synthase), C-terminal domain; 1.
DR SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR PROSITE; PS00533; PORPHOBILINOGEN_DEAM; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 3: Inferred from homology;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Coiled coil {ECO:0000256|SAM:Coils};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU10141}; Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000053240};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 50..487
FT /note="Protein kinase"
FT /evidence="ECO:0000259|PROSITE:PS50011"
FT REGION 805..829
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 905..928
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 761..788
FT /evidence="ECO:0000256|SAM:Coils"
FT COILED 860..887
FT /evidence="ECO:0000256|SAM:Coils"
FT COMPBIAS 813..829
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 912..928
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 85
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000256|PROSITE-ProRule:PRU10141"
SQ SEQUENCE 1458 AA; 165053 MW; B9A2BBE2129DDA7C CRC64;
MPRRGNEIET PITPKKKKVT EECASLDASF FDDEALPPGI VFTDVQSKKW RIGKPIGRGS
FGRIYLASNE VDKEVTKQNA RYVVKIEPHT NGPLFVEIHC LIRTAQASKV KTWCQENKLK
RLGMPIYIAS GSFTEESTGI KYRFLVLPRY DIDLQKIIAR TRTLDLKNVL VLSIQILDIL
EYLHNQGYTH SDIKSSNLMI GFDSNKVIKA TTPKSTQSFQ KNTKQVVLIP EKHKKPKTSR
SRSSNYYNDE DYVVSQRTPE ICKDDKRLVS VKNKLRKIFT EKDKGKLHRQ HAFNLRHLSN
YVNYEDLSSV CSDRSYQKLL DDFGNKSLLS VVETFKDGKK SENKDLELQM DQIYKDAILS
QSNGQIYLLD YGLASKFLDS KGNHKDFGMD ARKAHDGTLE YSSRDSHIGA HSRRSDLETL
GYNMLDWLTG TLPWKTSEVL ADPDLVHAVK KNFMNDIKTL LKTCFKTEFY PQFMEKYLQY
ITSLDFTEKP DYDYCRNLFK SEMIRNGYTF NREMNINFAE PSLSPISRSK LGYSKRFGRK
NTPPDFLSRN GIKKTYEREN VCSLENGLKL ELLKHTLNIS SEGVRKPCSS RNFFISDADL
VARLKKSLMP HDVLGKKLSP KNLRSKQKNM TKRKGARRHR NSIGKFGNLM GSARQFTWAE
ILAGNPEDII RKDRNPATNA DVEDDSTCKY RIRKLSNASS TNCDGSLQSP LMQKDYLQGL
NPTYAMKEVL ANFKKKLSGK TIKESEECPP GLEGYTPIMI KLHKLKEKRE AKEKLELLKQ
NSESKEFKKE PRCTRSMSNI ERPVRRSARN KPVNGGHVQT SDIRNSSEQV PVAIKSNDEI
KSPRTRSATN KKVVTIADTK KTAQTKKREA KEKLELLKQN SESKEFKKEP RCTRSMSNIE
RPVRRSARNK PVNGGHVQTS DIRNSSEQVP IAIKSNDEIK SPRTRSTTNK KGVTIADNKK
SAQTRTKTTT VVLNRRRLRS SKRKKSMESE KTNVVRVGSR KSELALIQTN FVIESLKKVY
PDKEFTIVSM TTLGDRILNV SLPKIGEKSL FTKDLEDALR NNSVDFVVHS LKDLPTTLPE
GLAIGAVFER EDPRDALVLR EELNTHTLST LPAGSVIGTS SLRRTAQLRG SYPQLSVIDV
RGNLNTRLKK LDAPSKEYSA LLLANAGLQR MGWGNRVSKI LPCSEIMYAV GQGALAVECR
SDNEDVLKML APFNHAETYC RVLAERSFLK TLVEGKDIQI LPCSEIMYAV GQGALAVECR
SDNEDVLKML APFNHPETYC RVLAERSFLK TLGGGCSAPV GVSTKLKHVD PQYKFTIEGA
VWSMDGTTKI HETLELVLPQ IKKTQKHKLS PTEESDCKKL KKENGAPKGL DAVLELNRRI
TERKDNLNCE DTRSMEEIAS LKCPIFCGLS ENSNIPIEVI EKCENLGKDL ANNLISKGAL
DVMKVTQDYI RSAAAQKS
//
