A2C7T6

PR
Gene name
chlN
Protein name
Light-independent protochlorophyllide reductase subunit N
Names
DPOR subunit N, LI-POR subunit N
Species
Prochlorococcus marinus (strain MIT 9303)
KEGG Pathway
pmf:P9303_07951
EC number
1.3.7.7: With an iron-sulfur protein as acceptor
Protein Class

Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

160-254 (Predicted disordered autoinhibitory region) PR

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

References

Autoinhibited structure

Activated structure

1 structures for A2C7T6

Entry ID Method Resolution Chain Position Source
AF-A2C7T6-F1 Predicted AlphaFoldDB

No variants for A2C7T6

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for A2C7T6

No associated diseases with A2C7T6

8 regional properties for A2C7T6

Type Name Position InterPro Accession
domain UVR domain 443 - 478 IPR001943
domain AAA+ ATPase domain 226 - 370 IPR003593-1
domain AAA+ ATPase domain 563 - 711 IPR003593-2
domain ATPase, AAA-type, core 231 - 364 IPR003959-1
domain ATPase, AAA-type, core 562 - 732 IPR003959-2
domain Clp, repeat (R) domain 2 - 145 IPR004176
domain Clp ATPase, C-terminal 739 - 829 IPR019489
domain ClpA/ClpB, AAA lid domain 369 - 470 IPR041546

Functions

Description
EC Number 1.3.7.7 With an iron-sulfur protein as acceptor
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

5 GO annotations of molecular function

Name Definition
4 iron, 4 sulfur cluster binding Binding to a 4 iron, 4 sulfur (4Fe-4S) cluster; this cluster consists of four iron atoms, with the inorganic sulfur atoms found between the irons and acting as bridging ligands.
ATP binding Binding to ATP, adenosine 5'-triphosphate, a universally important coenzyme and enzyme regulator.
metal ion binding Binding to a metal ion.
oxidoreductase activity, acting on iron-sulfur proteins as donors Catalysis of an oxidation-reduction (redox) reaction in which an iron-sulfur protein acts as a hydrogen or electron donor and reduces a hydrogen or electron acceptor.
oxidoreductase activity, acting on the CH-CH group of donors, iron-sulfur protein as acceptor Catalysis of an oxidation-reduction (redox) reaction in which a CH-CH group acts as a hydrogen or electron donor and reduces an iron-sulfur protein.

2 GO annotations of biological process

Name Definition
light-independent chlorophyll biosynthetic process The chemical reactions and pathways resulting in the formation of chlorophyll, any compound of magnesium complexed in a porphyrin (tetrapyrrole) ring and which functions as a photosynthetic pigment, from less complex precursors, which occur in the absence of light.
photosynthesis, dark reaction A complex cycle of enzyme-mediated reactions which catalyzes the reduction of carbon dioxide to sugar. As well as carbon dioxide the cycle requires reducing power in the form of reduced nicotinamide adenine dinucleotide phosphate (NADP) and chemical energy in the form of adenosine triphosphate (ATP). The reduced NADP (NADPH) and ATP are produced by the 'light' reactions.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MGSTTLLKES GPREVFCGLT SIVWLHRRMP DAFFLVVGSR TCAHLIQSAA GVMIFAEPRF
70 80 90 100 110 120
GTAILEERDL AGLADAHEEL DRVVNDLLAR RPEIRTLFLV GSCPSEVIKL DLARVAERLN
130 140 150 160 170 180
GQLQGGVRVL NYSGSGIETT FTQGEDGALK AMVPLMPNSN EAQLLLVGTM ANAVEDRLKH
190 200 210 220 230 240
LFERLGIPSV SSLPPRQSTD LPSVGPGTRV LLTQPYLTDT ARELKDRGAE ILQAPFPLGA
250 260 270 280 290 300
EGSRLWMEAA AQAFGINGSH VATILEPLMV RAQKALSPYK EQLAGKRIFL MPESQLEIPL
310 320 330 340 350 360
ARFLHRECGM ELVEVGVPYL NRDMMQSELE LLPPNTQVME GQHVEKQLDR VREQRPDLVV
370 380 390 400 410
CGMGLANPLE AEEIATKWSI ELIFSPIHGI DQAADLAELF ARPLHRRDLL NNQLLVSV