ID A0A0D1CLX2_USTMA Unreviewed; 1159 AA.
AC A0A0D1CLX2;
DT 29-APR-2015, integrated into UniProtKB/TrEMBL.
DT 29-APR-2015, sequence version 1.
DT 27-MAR-2024, entry version 43.
DE RecName: Full=Amine oxidase domain-containing protein {ECO:0000259|Pfam:PF01593};
GN ORFNames=UMAG_04236 {ECO:0000313|EMBL:KIS67738.1};
OS Ustilago maydis (strain 521 / FGSC 9021) (Corn smut fungus).
OC Eukaryota; Fungi; Dikarya; Basidiomycota; Ustilaginomycotina;
OC Ustilaginomycetes; Ustilaginales; Ustilaginaceae; Ustilago.
OX NCBI_TaxID=237631 {ECO:0000313|EMBL:KIS67738.1, ECO:0000313|Proteomes:UP000000561};
RN [1] {ECO:0000313|EMBL:KIS67738.1, ECO:0000313|Proteomes:UP000000561}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RX PubMed=17080091; DOI=10.1038/nature05248;
RA Kamper J., Kahmann R., Bolker M., Ma L.J., Brefort T., Saville B.J.,
RA Banuett F., Kronstad J.W., Gold S.E., Muller O., Perlin M.H., Wosten H.A.,
RA de Vries R., Ruiz-Herrera J., Reynaga-Pena C.G., Snetselaar K., McCann M.,
RA Perez-Martin J., Feldbrugge M., Basse C.W., Steinberg G., Ibeas J.I.,
RA Holloman W., Guzman P., Farman M., Stajich J.E., Sentandreu R.,
RA Gonzalez-Prieto J.M., Kennell J.C., Molina L., Schirawski J.,
RA Mendoza-Mendoza A., Greilinger D., Munch K., Rossel N., Scherer M.,
RA Vranes M., Ladendorf O., Vincon V., Fuchs U., Sandrock B., Meng S.,
RA Ho E.C., Cahill M.J., Boyce K.J., Klose J., Klosterman S.J., Deelstra H.J.,
RA Ortiz-Castellanos L., Li W., Sanchez-Alonso P., Schreier P.H.,
RA Hauser-Hahn I., Vaupel M., Koopmann E., Friedrich G., Voss H., Schluter T.,
RA Margolis J., Platt D., Swimmer C., Gnirke A., Chen F., Vysotskaia V.,
RA Mannhaupt G., Guldener U., Munsterkotter M., Haase D., Oesterheld M.,
RA Mewes H.W., Mauceli E.W., DeCaprio D., Wade C.M., Butler J., Young S.,
RA Jaffe D.B., Calvo S., Nusbaum C., Galagan J., Birren B.W.;
RT "Insights from the genome of the biotrophic fungal plant pathogen Ustilago
RT maydis.";
RL Nature 444:97-101(2006).
RN [2] {ECO:0000313|Proteomes:UP000000561}
RP GENOME REANNOTATION.
RC STRAIN=521 / FGSC 9021 {ECO:0000313|Proteomes:UP000000561};
RA Gueldener U., Muensterkoetter M., Walter M.C., Mannhaupt G., Kahmann R.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Catalyzes the 6-electron oxidation of protoporphyrinogen-IX
CC to form protoporphyrin-IX. {ECO:0000256|ARBA:ARBA00002600}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=3 O2 + protoporphyrinogen IX = 3 H2O2 + protoporphyrin IX;
CC Xref=Rhea:RHEA:25576, ChEBI:CHEBI:15379, ChEBI:CHEBI:16240,
CC ChEBI:CHEBI:57306, ChEBI:CHEBI:57307; EC=1.3.3.4;
CC Evidence={ECO:0000256|ARBA:ARBA00000672};
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginyl-[protein] + 2 S-adenosyl-L-methionine = 2 H(+) +
CC N(omega),N(omega)'-dimethyl-L-arginyl-[protein] + 2 S-adenosyl-L-
CC homocysteine; Xref=Rhea:RHEA:48108, Rhea:RHEA-COMP:10532, Rhea:RHEA-
CC COMP:11992, ChEBI:CHEBI:15378, ChEBI:CHEBI:29965, ChEBI:CHEBI:57856,
CC ChEBI:CHEBI:59789, ChEBI:CHEBI:88221; EC=2.1.1.320;
CC Evidence={ECO:0000256|ARBA:ARBA00000778};
CC -!- PATHWAY: Porphyrin-containing compound metabolism; protoporphyrin-IX
CC biosynthesis; protoporphyrin-IX from protoporphyrinogen-IX: step 1/1.
CC {ECO:0000256|ARBA:ARBA00005073}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion {ECO:0000256|ARBA:ARBA00004173}.
CC -!- SIMILARITY: Belongs to the NDUFAF7 family.
CC {ECO:0000256|ARBA:ARBA00005891}.
CC -!- SIMILARITY: Belongs to the protoporphyrinogen/coproporphyrinogen
CC oxidase family. Protoporphyrinogen oxidase subfamily.
CC {ECO:0000256|ARBA:ARBA00010551}.
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DR EMBL; CM003151; KIS67738.1; -; Genomic_DNA.
DR RefSeq; XP_011390712.1; XM_011392410.1.
DR AlphaFoldDB; A0A0D1CLX2; -.
DR STRING; 237631.A0A0D1CLX2; -.
DR EnsemblFungi; KIS67738; KIS67738; UMAG_04236.
DR GeneID; 23564483; -.
DR KEGG; uma:UMAG_04236; -.
DR VEuPathDB; FungiDB:UMAG_04236; -.
DR eggNOG; KOG1276; Eukaryota.
DR eggNOG; KOG2901; Eukaryota.
DR InParanoid; A0A0D1CLX2; -.
DR OMA; FYLARWQ; -.
DR OrthoDB; 166586at2759; -.
DR UniPathway; UPA00251; UER00324.
DR Proteomes; UP000000561; Chromosome 12.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0016705; F:oxidoreductase activity, acting on paired donors, with incorporation or reduction of molecular oxygen; IEA:UniProt.
DR GO; GO:0004729; F:oxygen-dependent protoporphyrinogen oxidase activity; IEA:UniProtKB-EC.
DR GO; GO:0035243; F:protein-arginine omega-N symmetric methyltransferase activity; IBA:GO_Central.
DR GO; GO:0032259; P:methylation; IEA:UniProtKB-KW.
DR GO; GO:0032981; P:mitochondrial respiratory chain complex I assembly; IBA:GO_Central.
DR GO; GO:0006782; P:protoporphyrinogen IX biosynthetic process; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.40.50.12710; -; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR002937; Amino_oxidase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR003788; NDUFAF7.
DR InterPro; IPR038375; NDUFAF7_sf.
DR InterPro; IPR004572; Protoporphyrinogen_oxidase.
DR InterPro; IPR029063; SAM-dependent_MTases_sf.
DR NCBIfam; TIGR00562; proto_IX_ox; 1.
DR PANTHER; PTHR12049:SF7; PROTEIN ARGININE METHYLTRANSFERASE NDUFAF7, MITOCHONDRIAL; 1.
DR PANTHER; PTHR12049; UNCHARACTERIZED; 1.
DR Pfam; PF01593; Amino_oxidase; 1.
DR Pfam; PF02636; Methyltransf_28; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF53335; S-adenosyl-L-methionine-dependent methyltransferases; 1.
PE 3: Inferred from homology;
KW Methyltransferase {ECO:0000256|ARBA:ARBA00022603};
KW Mitochondrion {ECO:0000256|ARBA:ARBA00023128};
KW Porphyrin biosynthesis {ECO:0000256|ARBA:ARBA00023244};
KW Reference proteome {ECO:0000313|Proteomes:UP000000561};
KW Transferase {ECO:0000256|ARBA:ARBA00022679}.
FT DOMAIN 47..580
FT /note="Amine oxidase"
FT /evidence="ECO:0000259|Pfam:PF01593"
FT REGION 604..628
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 652..680
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 963..989
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1159 AA; 126176 MW; 719DAF1445F6ABCE CRC64;
MLLTRTASRL QCLPRPAVTP NKALSSSTRA LATVTDKKYI AVLGGGISGL TSAYRLAQHL
PKDRYNIVLL EHQNRLGGWI RSERIVLPTA DGAAQNVTAL IEQGPRSIRP AGYSGLMMLE
LVRSLGLLER MLKVPKTAPS AQNRYLYYPD RLAKLPSSIP SLLSALFKLP FLRAIIPGVL
REPRVPSRFL RPRSESKSEK QRLQQREWIQ DESVDSFVSR RFGNGLAENL VSAVIHGIYA
GDTRKLSIRA VLPFLWEAER VHGSVLRSML STKRNKRHRA LPEPEAAVKA AKDLRLENIE
KELGKDVVES FKSISVYSFQ EGVQEIVQAL ESRLAEYDNV QIKKGDAVQS IHRNEAGKTT
LHTESGETMV VDRIISSIPS TRLAQILPSD AELPHLSHNP SANVGVVNLV ISPSAVASSS
KPLVPVEGFG YLIPRTSPGN QDGILGVVFD SDAIPEQDSV CAASRPVKLT VMMGGSHWAD
LETLPSEADM RARAINAVSQ HLGIDRSLLE DASKVSVRAT MQKDCIPWYL VGHPVRMSQL
HKALEKDELL GSKLTLVGAS YTGVSLNDCV AYATEAVEQI VDAELHGGER IVTGLASFAI
PPVPPSQKAT SITAQARKGD TRPSVNPQGL MGPITGTPNQ FAVAGSIHTR AFSTTRQKSN
SSSSSSSSSR STPVSSADKK TKSLNEILLD SIRASGPMPV STYMRTCLLD PMQGYYSSAN
SPSTSREVLG SRGDFITSPE ISQVFGELVA IFYLARWQSV GAPSATRIVE LGPGKGTLLA
DMLRTFATFK PFMATLKRIH LVETSEGLME LQLNAIKEAL GVVGKRVVSA EEDAGADGVV
VEWFPGIDMV PVIPEELTIL TAHEFFDALP THIFEKGVDG KFREVLVGIK PTSSITVLKP
GQDLQKQAQN EELGFVLSPT PTPWAQMLVQ NNPRFQHLEP GQRVEVSPEA WAVARRVGEI
VAGRSASAPS SPKQEAPRSA PEGSAEAKAE AALEAERLQA ERRLETQRLS HATEGGIGLI
IDYGDDKAYG SSLRAFKNHA LVRVFDSPGT VDLTVNVDFL HLKSAIHTTD ARYLGPIDQA
DFLVGMGLQM RTEALVKGRD AHDENRIKDA ANRLIDESGM GIQYKALAIT ARRCAENNAP
DQHRDKVADP DIYPFEFQH
//
