ID   COBN_PSEAE              Reviewed;        1248 AA.
AC   Q9HZQ3;
DT   15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2001, sequence version 1.
DT   03-AUG-2022, entry version 97.
DE   RecName: Full=Aerobic cobaltochelatase subunit CobN;
DE            EC=6.6.1.2;
DE   AltName: Full=Hydrogenobyrinic acid a,c-diamide cobaltochelatase subunit CobN;
GN   Name=cobN; OrderedLocusNames=PA2944;
OS   Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS   14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC   Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=208964;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC   PRS 101 / PAO1;
RX   PubMed=10984043; DOI=10.1038/35023079;
RA   Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA   Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA   Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA   Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA   Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA   Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT   "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT   pathogen.";
RL   Nature 406:959-964(2000).
CC   -!- FUNCTION: Catalyzes cobalt insertion in the corrin ring. {ECO:0000250}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + Co(2+) + H2O + hydrogenobyrinate a,c-diamide = ADP +
CC         cob(II)yrinate a,c diamide + 5 H(+) + phosphate;
CC         Xref=Rhea:RHEA:15341, ChEBI:CHEBI:15377, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:43474, ChEBI:CHEBI:48828,
CC         ChEBI:CHEBI:58537, ChEBI:CHEBI:77874, ChEBI:CHEBI:456216; EC=6.6.1.2;
CC   -!- PATHWAY: Cofactor biosynthesis; adenosylcobalamin biosynthesis;
CC       cob(II)yrinate a,c-diamide from precorrin-2 (aerobic route): step
CC       10/10.
CC   -!- SUBUNIT: Heterotrimer of CobN, CobS and CobT. {ECO:0000250}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- SIMILARITY: Belongs to the CobN family. {ECO:0000305}.
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DR   EMBL; AE004091; AAG06332.1; -; Genomic_DNA.
DR   PIR; G83278; G83278.
DR   RefSeq; NP_251634.1; NC_002516.2.
DR   RefSeq; WP_003113999.1; NZ_QZGE01000009.1.
DR   AlphaFoldDB; Q9HZQ3; -.
DR   SMR; Q9HZQ3; -.
DR   STRING; 287.DR97_4996; -.
DR   PaxDb; Q9HZQ3; -.
DR   PRIDE; Q9HZQ3; -.
DR   EnsemblBacteria; AAG06332; AAG06332; PA2944.
DR   GeneID; 882831; -.
DR   KEGG; pae:PA2944; -.
DR   PATRIC; fig|208964.12.peg.3088; -.
DR   PseudoCAP; PA2944; -.
DR   HOGENOM; CLU_002017_1_0_6; -.
DR   InParanoid; Q9HZQ3; -.
DR   OMA; WETGQAM; -.
DR   PhylomeDB; Q9HZQ3; -.
DR   BioCyc; PAER208964:G1FZ6-2995-MON; -.
DR   BRENDA; 6.6.1.2; 5114.
DR   UniPathway; UPA00148; UER00221.
DR   Proteomes; UP000002438; Chromosome.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0051116; F:cobaltochelatase activity; IEA:UniProtKB-EC.
DR   GO; GO:0009236; P:cobalamin biosynthetic process; IEA:UniProtKB-UniPathway.
DR   GO; GO:0006779; P:porphyrin-containing compound biosynthetic process; IEA:UniProtKB-KW.
DR   CDD; cd10150; CobN_like; 1.
DR   InterPro; IPR011953; Cobalto_CobN.
DR   InterPro; IPR003672; CobN/Mg_chltase.
DR   PANTHER; PTHR44119; PTHR44119; 1.
DR   Pfam; PF02514; CobN-Mg_chel; 1.
DR   TIGRFAMs; TIGR02257; cobalto_cobN; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Cobalamin biosynthesis; Cytoplasm; Ligase; Nucleotide-binding;
KW   Porphyrin biosynthesis; Reference proteome.
FT   CHAIN           1..1248
FT                   /note="Aerobic cobaltochelatase subunit CobN"
FT                   /id="PRO_0000287787"
SQ   SEQUENCE   1248 AA;  138501 MW;  C3D3DBFEE6736C7A CRC64;
     MHLLRTQPGG FVPDDGIAHL AQTPAELVIL CSGDSHLALL AEAARALPDD YPSLRLANPM
     QLQNHASVDL YVEEVLRHAR VILLSLHGGI GYWRYGVEQL VALAERGALL IPVPGDDRPD
     PELSALGNLP AEQAERFWQY LRQGGLENAG QFYRCLASQC LGRDYAWREP QALPRVALFH
     PRHAEATLEH WRADWQAGRP VVALLFYRTH LQAANTAFIA RFCERLAAQG LNPLPIALAS
     LKESACLAQV EDWLERSDAA LIVNTTGFAQ SNPEAPELRP FRRDVPVLQA ICSLDNRPLW
     LDNPQGLGPR DLAMHVALPE LDGRIVTRPI SFKGLAWRSE RSESDVVCYL ADDERMDFVA
     ELARRWAELA RKPNAEKRVA LVLANYPTRD GRIGNGVGLD TPAAALNILR ALRQQGYPVD
     GLPASGTELI RQLLGGVSND LEHLDLRPCA QSLALDDYLA CFARLPERNR QAVLARWGEP
     QQDPMFRDGR MMVAGLRYGL TFVGIQPARG YQLDPAAVYH DPDLVPPHGY LAFYFWLRHA
     YRADALLHVG KHGNLEWLPG KGVGLSAECW PDALLGPLPN IYPFIVNDPG EGAQAKRRTQ
     AVIIDHLMPP LTRAESYGPL RDLERLADEF YDASLLDPRR AEQLRGEILV LLRDNRLDRE
     IGLQLSDDPD SWLPQLDAYL CDLKESQIRD GLHVFGESPS GRLRLDTLLA LLRVPRGDGK
     GANAGLLKSL ADDLGLGFDP LACDMGEAWQ GARPACLEER GGEPWRTLGD TRERLELLAL
     HWIERCLGGE SPPATWRASG EVLRGLCEQV APTLDACGGA EIDGLLAALE GRFVPAGPSG
     APSRGRLDVL PTGRNFFSVD VRNLPTPTAW RIGFQSANLL LERHLQEHGD HLRQLGLSVW
     GTATMRTGGD DIAQALALLG VRPVWQAGSQ RVADFEILPV SLLDRPRVDV TLRVSGFFRD
     AFANLIRLFD AAVQAVAELD EAEELNPLAA RVRLERQRLE AQGTAPAEAR RQAGWRIFGA
     KPGAYGAGVQ GAIEERLWET RADLAEVYLN WGGYAYGAAD DGTPARERFA QRLERLQAVL
     HNQDNREHDL LDSNDYYQFQ GGMLAAVETL RGAPVASYHG DHSQPDNPRI RTLKEELNRV
     VRARAVNPKW IAGMKRHGYK GAFELAATVD YLCAFDATSE LIDDHQYALL ADAYLLDAET
     REFVRQHNPQ ALRDMAERLV EAQRRGLWQE PGAYREALEN LLLDVEEE